Evaluation of Cytoplasmic and Secreted Proteins of Staphylococcus aureus Revealed Adaptive Metabolic Homeostasis in Response to Adjustments within the Environmental Situations Consultant of the Human Wound Website
The pathogenesis of Staphylococcus aureus is principally attributed to its functionality to regulate to modifications in environmental situations, together with these current on human pores and skin or inside a wound web site. This examine investigated the modifications within the cytoplasmic and secreted proteins in S. aureus that occurred in response to alterations within the environmental parameters that might be discovered within the human wound web site.
In complete, sixty differentially regulated cytoplasmic proteins have been detected utilizing a label-free quantification strategy, and these proteins have been categorized into ten molecular capabilities: protein biosynthesis, glycolysis, sign transduction, metabolism, cell cycle, transport, vitality era, cell anchorage, nucleotide biosynthesis and unknown. These modifications represented attribute protein profiles when evaluated by principal part evaluation.
The bacterium responded to elevated NaCl at pH 6 by lowering the abundance of the vast majority of cytoplasmic proteins, whereas at pH eight there was a rise within the ranges of cytoplasmic proteins compared to the untreated cells.
The evaluation of the secreted proteins confirmed that there was a excessive diploma of distinction in each the depth and the distribution of many particular person protein bands in response to environmental challenges. From these outcomes, it was deduced that particular metabolic homeostasis occurred beneath every mixture of outlined environmental situations.
Coupling Ion Specificity of the Flagellar Stator Proteins MotA1/MotB1 of Paenibacillus sp. TCA20
The bacterial flagellar motor is a reversible rotary molecular nanomachine, which {couples} ion flux throughout the cytoplasmic membrane to torque era.
It contains a rotor and a number of stator complexes, and every stator complicated capabilities as an ion channel and determines the ion specificity of the motor. Though coupling ions for the motor rotation have been presumed to be solely monovalent cations, reminiscent of H+ and Na+, the stator complicated MotA1/MotB1 of Paenibacillus sp.
TCA20 (MotA1TCA/MotB1TCA) was reported to make use of divalent cations as coupling ions, reminiscent of Ca2+ and Mg2+. On this examine, we initially aimed to measure the motor torque generated by MotA1TCA/MotB1TCAbeneath the management of divalent cation driving force; nevertheless, we recognized that the coupling ion of MotA1TCAMotB1TCA may be very prone to be a monovalent ion.
We engineered a collection of useful chimeric stator proteins between MotB1TCAand Escherichia coli MotB. E. coli ΔmotAB cells expressing MotA1TCA and the chimeric MotB introduced vital motility within the absence of divalent cations.
Furthermore, we confirmed that MotA1TCA/MotB1TCA in Bacillus subtilis ΔmotABΔmotPS cells generates torque with out divalent cations.
Primarily based on two impartial experimental outcomes, we conclude that the MotA1TCA/MotB1TCA complicated instantly converts the vitality launched from monovalent cation flux to motor rotation.
rbprotein
HMOX2 Polyclonal Antibody
Description: A polyclonal antibody for detection of HMOX2 from Human, Mouse, Rat. This HMOX2 antibody is for WB, ELISA.
It’s affinity-purified from rabbit serum by affinity-chromatography utilizing the particular immunogenand is unconjugated. The antibody is produced in rabbit through the use of as an immunogen synthesized peptide derived from half area of human HMOX2 protein.
Anti-HMOX2 antibody
Description: Heme oxygenase, a necessary enzyme in heme catabolism, cleaves heme to kind biliverdin, which is subsequently transformed to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase exercise is induced by its substrate heme and by numerous nonheme substances.
Heme oxygenase happens as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase household. A number of alternatively spliced transcript variants encoding three totally different isoforms have been discovered for this gene.
Description: A polyclonal antibody against HMOX2. Recognizes HMOX2 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB;ELISA:1:1000-1:5000, WB:1:500-1:2000
Description: A polyclonal antibody against HMOX2. Recognizes HMOX2 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC, IF
Description: A polyclonal antibody for detection of HMOX2 from Human, Mouse, Rat. This HMOX2 antibody is for WB, ELISA. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human HMOX2 protein
Description: A polyclonal antibody for detection of HMOX2 from Human, Mouse, Rat. This HMOX2 antibody is for WB, ELISA. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human HMOX2 protein
Description: A polyclonal antibody for detection of HMOX2 from Human, Mouse, Rat. This HMOX2 antibody is for WB, ELISA. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human HMOX2 protein
Description: Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family. Several alternatively spliced transcript variants encoding three different isoforms have been found for this gene.
Description: Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong to the heme oxygenase family. Several alternatively spliced transcript variants encoding three different isoforms have been found for this gene.
Description: A polyclonal antibody raised in Goat that recognizes and binds to Human Goat Anti-HMOX2 . This antibody is tested and proven to work in the following applications:
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human HMOX2 (N-term). This antibody is tested and proven to work in the following applications:
Description: Description of target: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.;Species reactivity: Rat;Application: ;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 0.78U/L
Description: Description of target: HEME oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.;Species reactivity: Human;Application: ELISA;Assay info: ;Sensitivity: < 0.055ng/mL
Description: Description of target: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter. ;Species reactivity: Human;Application: ;Assay info: Assay Methodology: Quantitative Sandwich Immunoassay;Sensitivity: 0.08 ng/mL
Description: Staphylokinase Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 136 amino acids and having a molecular weight of 16kDa.;The Staphylokinase is purified by proprietary chromatographic methods.
Warmth shock protein 90 inhibitors block the antinociceptive results of opioids in mouse chemotherapy-induced neuropathy and most cancers bone ache fashions
Warmth shock protein 90 (Hsp90) is a ubiquitous sign transduction regulator, and Hsp90 inhibitors are in scientific improvement as most cancers therapeutics.
Nevertheless, there have been only a few research on the impression of Hsp90 inhibitors on ache or analgesia, a critical concern for most cancers sufferers. We beforehand discovered that Hsp90 inhibitors injected into the mind block opioid-induced antinociception in tail flick, paw incision, and HIV neuropathy ache.
This examine prolonged from that preliminary work to check the cancer-related scientific impression of Hsp90 inhibitors on opioid antinociception in cancer-induced bone ache in feminine BALB/c mice and chemotherapy-induced peripheral neuropathy in female and male CD-1 mice. Mice have been handled with Hsp90 inhibitors (17-AAG, KU-32) by the intracerebroventricular, intrathecal, or intraperitoneal routes, and after 24 hours, ache behaviors have been evaluated after analgesic drug therapy.
Warmth shock protein 90 inhibition within the mind or systemically utterly blocked morphine and oxymorphone antinociception in chemotherapy-induced peripheral neuropathy; this impact was partly mediated by decreased ERK and JNK MAPK activation and by elevated protein translation, was not altered by power therapy, and Hsp90 inhibition had no impact on gabapentin antinociception.
We additionally discovered that the Hsp90 isoform Hsp90α and the cochaperone Cdc37 have been answerable for the noticed modifications in opioid antinociception. Against this, Hsp90 inhibition within the spinal twine or systemically partially decreased opioid antinociception in cancer-induced bone ache.
These outcomes reveal that Hsp90 inhibitors block opioid antinociception in cancer-related ache, suggesting that Hsp90 inhibitors for most cancers remedy may lower opioid therapy efficacy
Description: FAM3C, also called interleukin-like EMT inducer, usually exist in most secretory epithelia. It belongs to the FAM3 family according to their sequence similarities. The up-regulation and/or mislocalization in breast cancer and liver carcinoma cells of FAM3C is strongly correlated with metastasis formation and survival. FAM3C can be involved in retinal laminar formation and promote epithelial to mesenchymal transition.
Description: Protein FAM3D is a novel cytokine-like protein that belongs to the FAM3 family. Human FAM3D is synthesized as a 224 amino acid precursor that contains a 25 amino acid signal sequence and a 199 amino acid mature chain. FAM3D is identified based on structural, but not sequence, homology to short chain cytokines including IL-2, IL-4 and GM-CSF. FAM3 proteins are four helix bundle cytokines with four conserved cysteines in all members (FAM3A-D). FAM3B is highly expressed in alpha and beta cells of the pancreas and is being investigated as a potential contributor to beta cell death and development of Type I Diabetes.
Description: Protein G is an immunoglobulin-binding protein expressed in group C and G Streptococcal bacteria much like Protein A but with differing specificities. It is a 65-kDa (G148 protein G) and a 58 kDa (C40 protein G) cell surface protein that has found application in purifying antibodies through its binding to the Fc region. The native molecule also binds albumin, however, because serum albumin is a major contaminant of antibody sources, the albumin binding site has been removed from this recombinant form of Protein G.
Description: Protein L was isolated from the surface of bacterial species Peptostreptococcus magnus and was found to bind Ig(IgG,IgM,IgA,IgE and IgD) through L chain interaction, from which the name was suggested. Despite this wide-ranging binding capability with respect to Ig classes, Protein L is not a universal immunoglobilin-binding protein. Binding of Protein L to immunoglobulins is restricted to those containing kappa light chains (i.e., k chain of the VL domain). In humans and mice, kappa (k) light chains predominate. The remaining immunoglobulins have lambda (l) light chains. The recombinant protein contains four immunoglobulin (Ig) binding domains (Bdomains) of the native protein. Besides antibody, protein L is also suitable for binding of a wide range of antibody fragments such as Fabs, single-chain variable fragments (scFv), and domain antibodies (Dabs).
Description: Survivin is a member of the inhibitor of apoptosis protein (IAP) family, that has been implicated in both control of cell division and inhibition of apoptosis.
Description: Protein p62 preferentially binds multiubiquitin chains and forms a novel cytoplasmic structure "sequestosome" which serves as a storage place for ubiquitinated proteins.
Description: CXCL4 is a CXC chemokine that is expressed in megakaryocytes and stored in the alpha-granules of platelets. CXCL4 is chemotactic towards neutrophils and monocytes and has been shown to inhibit angiogenesis. Recombinant human CXCL4 is a 7.8 kDa protein containing 70 amino acid residues, including the four highly conserved residues present in CXC chemokines.
Description: CXCL4 is a CXC chemokine that is expressed in megakaryocytes and stored in the alpha-granules of platelets. CXCL4 is chemotactic towards neutrophils and monocytes and has been shown to inhibit angiogenesis. Recombinant human CXCL4 is a 7.8 kDa protein containing 70 amino acid residues, including the four highly conserved residues present in CXC chemokines.
Description: CXCL8 (IL-8) is a proinflammatory CXC chemokine that can signal through the CXCR1 and CXCR2 receptors. It is secreted by monocytes and endothelial cells. CXCL8 (IL-8) chemoattracts and activates neutrophils. Recombinant human CXCL8 (IL-8) (endothelial-derived) is an 8.9 kDa protein containing 77 amino acid residues.
Description: CXCL8 (IL-8) is a proinflammatory CXC chemokine that can signal through the CXCR1 and CXCR2 receptors. It is secreted by monocytes and endothelial cells. CXCL8 (IL-8) chemoattracts and activates neutrophils. Recombinant human CXCL8 (IL-8) (endothelial-derived) is an 8.9 kDa protein containing 77 amino acid residues.
Description: BCMA, a member of the TNF receptor superfamily, binds to BAFF and APRIL. BCMA is expressed on mature B-cells and other B-cell lines and plays an important role in B cell development, function and regulation. BCMA also has the capability to activate NF-kappaB and JNK. The human BCMA gene codes for a 184 amino acid type I transmembrane protein, which contains a 54 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 107 amino acid extracellular domain. Recombinant soluble BCMA is a 50 amino acid polypeptide (5.3 kDa) comprising the TNFR homologous region of the BCMA protein.
Description: BCMA, a member of the TNF receptor superfamily, binds to BAFF and APRIL. BCMA is expressed on mature B-cells and other B-cell lines and plays an important role in B cell development, function and regulation. BCMA also has the capability to activate NF-kappaB and JNK. The human BCMA gene codes for a 184 amino acid type I transmembrane protein, which contains a 54 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 107 amino acid extracellular domain. Recombinant soluble BCMA is a 50 amino acid polypeptide (5.3 kDa) comprising the TNFR homologous region of the BCMA protein.
Description: Visfatin is a 55 kDa protein produced and secreted primarily by white adipose tissue. Recently, Visfatin was isolated from visceral fat deposits and shown to possess insulin-mimetic activity. Like insulin, Visfatin exerts hypoglycemic effects by interacting with the insulin receptor. The binding affinity of Visfatin for the insulin receptor is similar to that of insulin, but it does not compete with insulin, suggesting that the two proteins interact with different receptor sites. The circulating levels of Visfatin are much lower than those of insulin and are not affected by feeding, implying that the hypoglycemic effect of Visfatin may not be of physiological importance. The plasma Visfatin levels, like those of Leptin, correlate positively with the percent of body fat and increase during the development of obesity. Another similarity between Visfatin and Leptin is that their amino acid sequence is highly conserved across different mammalian species and shows no homology to any known protein. Receptors for both Leptin (Ob-R) and Visfatin (i.e. the insulin receptor) are expressed by neurons within the arcuate nucleus of the hypothalamus, a brain area that plays a pivotal role in the regulation of energy metabolism. Although the metabolic function of Visfatin is still unknown, it appears that this newly identified adipocytokine might play an important role, similar to that of Leptin, in the regulation of body weight, i.e. as an afferent signal reflecting excess body fat. Recombinant human Visfatin is a 52.5 kDa protein containing 465 amino acid residues (isoform 1).
Description: Visfatin is a 55 kDa protein produced and secreted primarily by white adipose tissue. Recently, Visfatin was isolated from visceral fat deposits and shown to possess insulin-mimetic activity. Like insulin, Visfatin exerts hypoglycemic effects by interacting with the insulin receptor. The binding affinity of Visfatin for the insulin receptor is similar to that of insulin, but it does not compete with insulin, suggesting that the two proteins interact with different receptor sites. The circulating levels of Visfatin are much lower than those of insulin and are not affected by feeding, implying that the hypoglycemic effect of Visfatin may not be of physiological importance. The plasma Visfatin levels, like those of Leptin, correlate positively with the percent of body fat and increase during the development of obesity. Another similarity between Visfatin and Leptin is that their amino acid sequence is highly conserved across different mammalian species and shows no homology to any known protein. Receptors for both Leptin (Ob-R) and Visfatin (i.e. the insulin receptor) are expressed by neurons within the arcuate nucleus of the hypothalamus, a brain area that plays a pivotal role in the regulation of energy metabolism. Although the metabolic function of Visfatin is still unknown, it appears that this newly identified adipocytokine might play an important role, similar to that of Leptin, in the regulation of body weight, i.e. as an afferent signal reflecting excess body fat. Recombinant human Visfatin is a 52.5 kDa protein containing 465 amino acid residues (isoform 1).
Description: Artemin is a disulfide-linked homodimeric neurotrophic factor structurally related to GDNF, Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. Artemin, GDNF, Persephin and Neurturin all signal through a multicomponent receptor system, composed of RET (receptor tyrosine kinase) and one of the four GFRalpha (alpha1-alpha4) receptors. Artemin prefers the receptor GFRalpha3-RET, but will use other receptors as an alternative. Artemin supports the survival of all peripheral ganglia such as sympathetic, neural crest and placodally derived sensory neurons, and dompaminergic midbrain neurons. The functional human Artemin ligand is a disulfide-linked homodimer, of two 12.0 kDa polypeptide monomers. Each monomer contains seven conserved cysteine residues, one of which is used for interchain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine knot configuration. Recombinant human Artemin is a 24.2 kDa, disulfide-linked homodimer formed by two identical 113 amino acid subunits.
Description: Artemin is a disulfide-linked homodimeric neurotrophic factor structurally related to GDNF, Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. Artemin, GDNF, Persephin and Neurturin all signal through a multicomponent receptor system, composed of RET (receptor tyrosine kinase) and one of the four GFRalpha (alpha1-alpha4) receptors. Artemin prefers the receptor GFRalpha3-RET, but will use other receptors as an alternative. Artemin supports the survival of all peripheral ganglia such as sympathetic, neural crest and placodally derived sensory neurons, and dompaminergic midbrain neurons. The functional human Artemin ligand is a disulfide-linked homodimer, of two 12.0 kDa polypeptide monomers. Each monomer contains seven conserved cysteine residues, one of which is used for interchain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine knot configuration. Recombinant human Artemin is a 24.2 kDa, disulfide-linked homodimer formed by two identical 113 amino acid subunits.
Description: Sox2, also known as sex determining region Y (SRY)-box 2, belongs to a diverse family of structurally-related transcription factors whose primary structure contains a 79-residue DNA-binding domain, called high mobility group (HMG) box. It plays an essential role in maintaining the pluripotency of embryonic stem cells (ESC) and determination of cell fate. Microarray analysis showed that Sox2 regulates the expression of multiple genes involved in embryonic development including FGF-4, YES1 and ZFP206. Sox2 acts as a transcriptional activator after forming a ternary complex with Oct3/4 and a conserved non-coding DNA sequence (CNS1) located approximately 2 kb upstream of the RAX promoter. The introduction of Sox2, Oct4, Myc, and Klf4, into human dermal fibroblasts isolated from a skin biopsy of a healthy research fellow was sufficient to confer a pluripotent state upon the fibroblast genome. The reprogrammed cells thus obtained resemble ESC in morphology, gene expression, and in the capacity to form teratomas in immune-deficient mice. Recombinant human Sox2 is a 34.3 kDa protein containing 317 amino-acid residues.
Description: Sox2, also known as sex determining region Y (SRY)-box 2, belongs to a diverse family of structurally-related transcription factors whose primary structure contains a 79-residue DNA-binding domain, called high mobility group (HMG) box. It plays an essential role in maintaining the pluripotency of embryonic stem cells (ESC) and determination of cell fate. Microarray analysis showed that Sox2 regulates the expression of multiple genes involved in embryonic development including FGF-4, YES1 and ZFP206. Sox2 acts as a transcriptional activator after forming a ternary complex with Oct3/4 and a conserved non-coding DNA sequence (CNS1) located approximately 2 kb upstream of the RAX promoter. The introduction of Sox2, Oct4, Myc, and Klf4, into human dermal fibroblasts isolated from a skin biopsy of a healthy research fellow was sufficient to confer a pluripotent state upon the fibroblast genome. The reprogrammed cells thus obtained resemble ESC in morphology, gene expression, and in the capacity to form teratomas in immune-deficient mice. Recombinant human Sox2 is a 34.3 kDa protein containing 317 amino-acid residues.
Description: Nanog is a regulatory protein that is associated with undifferentiated pluripotent cells. The expression of Nanog, which is suppressed in all adult tissues, is restricted to embryonic stem cells and to certain pluripotent cancer cells. Decreased expression of Nanog is strongly correlated with cell differentiation. Nanog, most likely, acts as an intracellular regulator, which maintains pluripotency and self renewal via a STAT3 independent pathway. Recombinant human Nanog is a 34.5 kDa protein, which is synthesized as a 304 amino acid polypeptide lacking a signal sequence for secretion.
Description: Nanog is a regulatory protein that is associated with undifferentiated pluripotent cells. The expression of Nanog, which is suppressed in all adult tissues, is restricted to embryonic stem cells and to certain pluripotent cancer cells. Decreased expression of Nanog is strongly correlated with cell differentiation. Nanog, most likely, acts as an intracellular regulator, which maintains pluripotency and self renewal via a STAT3 independent pathway. Recombinant human Nanog is a 34.5 kDa protein, which is synthesized as a 304 amino acid polypeptide lacking a signal sequence for secretion.
Description: Osteopontin is a secreted glycoprotein that functions as a ligand to alphavbeta3 integrin and possibly other receptors. It binds tightly to hydroxyapatite and can act as a structural component of the extracellular mineralized matrix. Osteopontin is initially secreted as a 298 amino acid protein, which is subject to multiple post-translational modifications including glycosylation, phosphorylation, and specific proteolytic cleavages into various smaller molecular weight fragments. Osteopontin is expressed in a wide range of cells and tissues including osteoblasts, various tumor cell lines, extraosseous cells in the inner ear, brain, kidney, deciduum, placenta and odontoblasts. In addition to its involvement in mineralized matrix formation, Osteopontin can also function as a cytokine that stimulates the release of IFNγ and IL-12, while inhibiting the production of IL-10. Recombinant human Osteopontin is a 298 amino acid protein, which, due to glycosylation, migrates at an apparent molecular weight of 60.0-65.0 kDa by SDS-PAGE analysis under reducing conditions.
Description: Osteopontin is a secreted glycoprotein that functions as a ligand to alphavbeta3 integrin and possibly other receptors. It binds tightly to hydroxyapatite and can act as a structural component of the extracellular mineralized matrix. Osteopontin is initially secreted as a 298 amino acid protein, which is subject to multiple post-translational modifications including glycosylation, phosphorylation, and specific proteolytic cleavages into various smaller molecular weight fragments. Osteopontin is expressed in a wide range of cells and tissues including osteoblasts, various tumor cell lines, extraosseous cells in the inner ear, brain, kidney, deciduum, placenta and odontoblasts. In addition to its involvement in mineralized matrix formation, Osteopontin can also function as a cytokine that stimulates the release of IFNγ and IL-12, while inhibiting the production of IL-10. Recombinant human Osteopontin is a 298 amino acid protein, which, due to glycosylation, migrates at an apparent molecular weight of 60.0-65.0 kDa by SDS-PAGE analysis under reducing conditions.
Description: Neuroserpin is an inhibitory serpin that is expressed predominantly in central nervous system. Although the physiological target of neuroserpin is still unclear, cumulative evidence suggest that it plays an important role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. In the adult brain, neuroserpin is secreted from the growth cones of neurons in areas where synaptic changes are associated with learning and memory, i.e. cerebral cortex, hippocampus, and amygdala. The neuroprotective role of neuroserpin has been demonstrated in transgenic mice lacking neuroserpin expression. The deficiency of neuroserpin in these mice was associated with motor neuron disease characterized by axonal degradation. In humans, defects in neuroserpin, caused by point mutations in the neuroserpin gene, underlie a hereditary disorder called the familial encephalopathy with neuroserpin inclusion bodies (FENIB). Recombinant human neuroserpin is a 44.6 kDa non-glycosylated protein containing 394 amino-acid residues.
Description: Neuroserpin is an inhibitory serpin that is expressed predominantly in central nervous system. Although the physiological target of neuroserpin is still unclear, cumulative evidence suggest that it plays an important role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. In the adult brain, neuroserpin is secreted from the growth cones of neurons in areas where synaptic changes are associated with learning and memory, i.e. cerebral cortex, hippocampus, and amygdala. The neuroprotective role of neuroserpin has been demonstrated in transgenic mice lacking neuroserpin expression. The deficiency of neuroserpin in these mice was associated with motor neuron disease characterized by axonal degradation. In humans, defects in neuroserpin, caused by point mutations in the neuroserpin gene, underlie a hereditary disorder called the familial encephalopathy with neuroserpin inclusion bodies (FENIB). Recombinant human neuroserpin is a 44.6 kDa non-glycosylated protein containing 394 amino-acid residues.
Description: ApoE3 belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. E3 is the most common isoform and is present in 40-90% of the population. Recombinant human ApoE3 is a 34.4 kDa protein containing 300 amino acid residues.
Description: ApoE3 belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. E3 is the most common isoform and is present in 40-90% of the population. Recombinant human ApoE3 is a 34.4 kDa protein containing 300 amino acid residues.
Description: ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Individuals heterozygous for the ApoE4 allele are at higher risk of late-onset Alzheimer’s disease. Recombinant human ApoE4 is a 34.4 kDa protein containing 300 amino acid residues.
Description: ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Individuals heterozygous for the ApoE4 allele are at higher risk of late-onset Alzheimer’s disease. Recombinant human ApoE4 is a 34.4 kDa protein containing 300 amino acid residues.
Description: ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE is an important constituent of all plasma lipoproteins. It’s interaction with specific ApoE receptor enables uptake of chylomicron remnants by liver cells, which is an essential step during normal lipid metabolism. It also binds with the LDL receptor (apo B/E). Defects in ApoE are a cause of hyperlipoproteinemia type III. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Compared with E3 and E4, E2 exhibits the lowest receptor binding affinity. E2 allele carriers had significantly lower levels of total cholesterol, low-density lipoprotein cholesterol, and non-high-density lipoprotein cholesterol, as well as increased ApoE levels. Recombinant human ApoE2 is a 34.3 kDa protein containing 300 amino acid residues.
Description: ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE is an important constituent of all plasma lipoproteins. It’s interaction with specific ApoE receptor enables uptake of chylomicron remnants by liver cells, which is an essential step during normal lipid metabolism. It also binds with the LDL receptor (apo B/E). Defects in ApoE are a cause of hyperlipoproteinemia type III. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Compared with E3 and E4, E2 exhibits the lowest receptor binding affinity. E2 allele carriers had significantly lower levels of total cholesterol, low-density lipoprotein cholesterol, and non-high-density lipoprotein cholesterol, as well as increased ApoE levels. Recombinant human ApoE2 is a 34.3 kDa protein containing 300 amino acid residues.
Description: CD22 is a B-lineage restricted 135 kDa glycoprotein whose cell surface expression is limited to resting and activated B lymphocytes. The physiological role of CD22 is still unknown. Targeted disruption of CD22 in mice results in a reduced level of surface IgM on peripheral B cells suggesting a role for CD22 in limiting antigen receptor signaling. CD22 is a member of the Ig gene superfamily that uniquely binds a sialic acid-dependent ligand. Recombinant human CD22 is a soluble 75.0 kDa protein which corresponds to the extracellular domain of CD22.
Description: CD22 is a B-lineage restricted 135 kDa glycoprotein whose cell surface expression is limited to resting and activated B lymphocytes. The physiological role of CD22 is still unknown. Targeted disruption of CD22 in mice results in a reduced level of surface IgM on peripheral B cells suggesting a role for CD22 in limiting antigen receptor signaling. CD22 is a member of the Ig gene superfamily that uniquely binds a sialic acid-dependent ligand. Recombinant human CD22 is a soluble 75.0 kDa protein which corresponds to the extracellular domain of CD22.
Description: Epiregulin is an EGF related growth factor that binds specifically to EGFR (ErbB1) and ErbB4, but not ErbB2 or ErbB3. It is expressed mainly in the placenta and peripheral blood leukocytes and in certain carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. It also inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence. Recombinant human Epiregulin is a 5.6 kDa monomeric protein, containing 50 amino residues, which corresponds to the mature secreted Epiregulin sequence.
Description: Epiregulin is an EGF related growth factor that binds specifically to EGFR (ErbB1) and ErbB4, but not ErbB2 or ErbB3. It is expressed mainly in the placenta and peripheral blood leukocytes and in certain carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. It also inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence. Recombinant human Epiregulin is a 5.6 kDa monomeric protein, containing 50 amino residues, which corresponds to the mature secreted Epiregulin sequence.
Description: Prolactin is a neuroendocrine hormone secreted by the pituitary gland. Its primary function is to promote and maintain lactation during pregnancy and suckling. In addition, Prolactin plays an immune-regulatory role by stimulating the activities of ornithine decarboxylase and protein kinase C, which are important for the proliferation, differentiation, and function of lymphocytes. Recombinant human Prolactin is a 23 kDa globular protein containing 200 amino acid residues.
Description: Prolactin is a neuroendocrine hormone secreted by the pituitary gland. Its primary function is to promote and maintain lactation during pregnancy and suckling. In addition, Prolactin plays an immune-regulatory role by stimulating the activities of ornithine decarboxylase and protein kinase C, which are important for the proliferation, differentiation, and function of lymphocytes. Recombinant human Prolactin is a 23 kDa globular protein containing 200 amino acid residues.
Description: PTHrP is a polypeptide hormone produced by almost every tissue of the body. PTHrP is closely related to parathyroid hormone (PTH), which is secreted from the parathyroid gland, and plays a central role in regulating the extracellular concentrations of calcium and phosphorous. Recombinant human PTHrP is a 9.8 kDa linear polypeptide of 86 amino acid residues.
Description: PTHrP is a polypeptide hormone produced by almost every tissue of the body. PTHrP is closely related to parathyroid hormone (PTH), which is secreted from the parathyroid gland, and plays a central role in regulating the extracellular concentrations of calcium and phosphorous. Recombinant human PTHrP is a 9.8 kDa linear polypeptide of 86 amino acid residues.
Description: Keratinocyte Growth Factor (KGF/FGF-7) is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development and postnatal growth and regeneration of variety of tissues, by promoting cellular proliferation and differentiation. KGF/FG-7 is a mitogen factor specific for epithelial cells and keratinocytes and signals through FGFR 2b. KGF/FGF-7 plays a role in kidney and lung development, angiogenesis, and wound healing. Recombinant human KGF/FGF-7 is an 18.9 kDa protein consisting of 163 amino acid residues.
Description: Keratinocyte Growth Factor (KGF/FGF-7) is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development and postnatal growth and regeneration of variety of tissues, by promoting cellular proliferation and differentiation. KGF/FG-7 is a mitogen factor specific for epithelial cells and keratinocytes and signals through FGFR 2b. KGF/FGF-7 plays a role in kidney and lung development, angiogenesis, and wound healing. Recombinant human KGF/FGF-7 is an 18.9 kDa protein consisting of 163 amino acid residues.
Description: VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. Substantial evidence implicates VEGF in the induction of tumor metastasis and intra-ocular neovascular syndromes. VEGF signals through the three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Recombinant human VEGF165 is a 38.2 kDa disulfide-linked homodimeric protein consisting of two 165 amino acid polypeptide chains.
Description: VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. Substantial evidence implicates VEGF in the induction of tumor metastasis and intra-ocular neovascular syndromes. VEGF signals through the three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Recombinant human VEGF165 is a 38.2 kDa disulfide-linked homodimeric protein consisting of two 165 amino acid polypeptide chains.
Description: VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. VEGF signals through three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Due to its increased acidity, VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates. Recombinant human VEGF121 is a 28.4 kDa disulfide-linked homodimeric protein consisting of two 121 amino acid polypeptide chains.
Description: VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. VEGF signals through three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Due to its increased acidity, VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates. Recombinant human VEGF121 is a 28.4 kDa disulfide-linked homodimeric protein consisting of two 121 amino acid polypeptide chains.
Description: HGF is a mesenchymally derived potent mitogen for mature parenchymal hepatocyte cells and acts as a growth factor for a broad spectrum of tissues and cell types. HGF signals through a transmembrane tyrosine kinase receptor known as MET. Activities of HGF include induction of cell proliferation, motility, morphogenesis, inhibition of cell growth, and enhancement of neuron survival. HGF is a crucial mitogen for liver regeneration processes, especially after partial hepatectomy and other liver injuries. Human and murine HGF are cross-reactive. Human HGF is expressed as a linear 697 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of HGF, which consists of two polypeptide chains (α-chain and β-chain) held by a single disulfide bond resulting in formation of a biologically active heterodimer. The α-chain consists of 463 amino acid residues and four kringle domains. The β-chain consists of 234 amino acid residues.
Description: HGF is a mesenchymally derived potent mitogen for mature parenchymal hepatocyte cells and acts as a growth factor for a broad spectrum of tissues and cell types. HGF signals through a transmembrane tyrosine kinase receptor known as MET. Activities of HGF include induction of cell proliferation, motility, morphogenesis, inhibition of cell growth, and enhancement of neuron survival. HGF is a crucial mitogen for liver regeneration processes, especially after partial hepatectomy and other liver injuries. Human and murine HGF are cross-reactive. Human HGF is expressed as a linear 697 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of HGF, which consists of two polypeptide chains (α-chain and β-chain) held by a single disulfide bond resulting in formation of a biologically active heterodimer. The α-chain consists of 463 amino acid residues and four kringle domains. The β-chain consists of 234 amino acid residues.
Description: Members of the Hedgehog (Hh) family are highly conserved proteins which are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh) are structurally related and share a high degree of amino-acid sequence identity (e.g., Shh and Ihh are 93% identical). The biologically active form of Hh molecules is obtained by autocatalytic cleavage of their precursor proteins and corresponds to approximately the N-terminal one half of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can substitute for each other in experimental systems. Recombinant E. coli derived Human Sonic HedgeHog is a 20.0 kDa protein consisting of 176 amino acid residues, including an N-terminal Ile-Val-Ile sequence substituted for the natural occurring chemically modified Cys residue.
Description: Members of the Hedgehog (Hh) family are highly conserved proteins which are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh) are structurally related and share a high degree of amino-acid sequence identity (e.g., Shh and Ihh are 93% identical). The biologically active form of Hh molecules is obtained by autocatalytic cleavage of their precursor proteins and corresponds to approximately the N-terminal one half of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can substitute for each other in experimental systems. Recombinant E. coli derived Human Sonic HedgeHog is a 20.0 kDa protein consisting of 176 amino acid residues, including an N-terminal Ile-Val-Ile sequence substituted for the natural occurring chemically modified Cys residue.
Description: Betacellulin is an EGF-related polypeptide growth factor that signals through the EGF receptor. It is produced in several tissues, including the pancreas, small intestine, and in certain tumor cells. Betacellulin is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. Human Betacellulin is initially synthesized as a glycosylated 32.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce the mature sequence. Recombinant human Betacellulin is a 9.0 kDa monomeric protein, containing 80 amino residues, which comprises the mature EGF homologous portion of the Betacellulin protein.
Description: Betacellulin is an EGF-related polypeptide growth factor that signals through the EGF receptor. It is produced in several tissues, including the pancreas, small intestine, and in certain tumor cells. Betacellulin is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. Human Betacellulin is initially synthesized as a glycosylated 32.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce the mature sequence. Recombinant human Betacellulin is a 9.0 kDa monomeric protein, containing 80 amino residues, which comprises the mature EGF homologous portion of the Betacellulin protein.
Description: Epigen is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. It is produced in several tissues, including the testis, liver, heart and in certain tumor cells. Epigen is mitogenic for fibroblasts and epithelial cells. Human Epigen is initially synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence. Recombinant human Epigen is a 7.9kDa monomeric protein, containing 72 amino acid residues, which comprises the EGF homologous portion of the Epigen precursor.
Description: Epigen is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. It is produced in several tissues, including the testis, liver, heart and in certain tumor cells. Epigen is mitogenic for fibroblasts and epithelial cells. Human Epigen is initially synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence. Recombinant human Epigen is a 7.9kDa monomeric protein, containing 72 amino acid residues, which comprises the EGF homologous portion of the Epigen precursor.
Description: Klotho is a glycosylated protein that plays an important role in the regulation of phosphate and calcium homeostasis. The full length transmembrane form has a large extracellular domain composed of two homologous subunits termed KL1 and KL2, which contain 516 and 439 amino acid residues, respectively, The predominant circulating form, which is derived from alternative RNA splicing, contains the KL1 subunit and constitutes the N-terminal sequence of transmembrane Klotho. A third Klotho protein of about 128 kDa has been identified in the blood and cerebrospinal fluid. This circulating protein arises from the action of an as yet unidentified protease which cleaves transmembrane Klotho just above and/or within the plasma membrane. Klotho has been shown to play a key role in the signaling cascade of fibroblast growth factor-23 (FGF-23), a bone derived hormone that acts in the kidney to inhibit phosphate reabsorption and vitamin D biosynthesis. Klotho promotes FGF-23 signaling through binding to FGFRI (IIIc) which converts this canonical FGF receptor into a specific receptor for FGF-23. In the absence of Klotho the function of FGF-23 is literally abolished. Recombinant human Klotho is a 65-70 kDa glycoprotein containing 516 amino acid residues.
Description: Klotho is a glycosylated protein that plays an important role in the regulation of phosphate and calcium homeostasis. The full length transmembrane form has a large extracellular domain composed of two homologous subunits termed KL1 and KL2, which contain 516 and 439 amino acid residues, respectively, The predominant circulating form, which is derived from alternative RNA splicing, contains the KL1 subunit and constitutes the N-terminal sequence of transmembrane Klotho. A third Klotho protein of about 128 kDa has been identified in the blood and cerebrospinal fluid. This circulating protein arises from the action of an as yet unidentified protease which cleaves transmembrane Klotho just above and/or within the plasma membrane. Klotho has been shown to play a key role in the signaling cascade of fibroblast growth factor-23 (FGF-23), a bone derived hormone that acts in the kidney to inhibit phosphate reabsorption and vitamin D biosynthesis. Klotho promotes FGF-23 signaling through binding to FGFRI (IIIc) which converts this canonical FGF receptor into a specific receptor for FGF-23. In the absence of Klotho the function of FGF-23 is literally abolished. Recombinant human Klotho is a 65-70 kDa glycoprotein containing 516 amino acid residues.
Description: Myostatin is a TGF-beta family member that acts as an inhibitor of skeletal muscle growth. This muscle-specific cytokine interacts with Activin type I and type II receptors, and suppresses myoblast proliferation by arresting cell-cycle in the G1 phase. Suppression of myostatin activity facilitates muscle formation and may be useful in reducing and/or preventing adiposity and type-2 diabetes. Myostatin activity can be blocked by the Activin-binding protein Follistatin, and by the propeptide of Myostatin. Recombinant Human myostatin is a 25.0 kDa protein consisting of two identical 109 amino acid polypeptides linked by a single disulfide bond.
Description: Myostatin is a TGF-beta family member that acts as an inhibitor of skeletal muscle growth. This muscle-specific cytokine interacts with Activin type I and type II receptors, and suppresses myoblast proliferation by arresting cell-cycle in the G1 phase. Suppression of myostatin activity facilitates muscle formation and may be useful in reducing and/or preventing adiposity and type-2 diabetes. Myostatin activity can be blocked by the Activin-binding protein Follistatin, and by the propeptide of Myostatin. Recombinant Human myostatin is a 25.0 kDa protein consisting of two identical 109 amino acid polypeptides linked by a single disulfide bond.
Description: Twisted Gastrulation Protein (TSG) is a secreted BMP binding protein structurally related to the BMP antagonists Chordin and Noggin. TSG can inhibit BMP activity by binding directly to BMP proteins, and can act either as a BMP4 agonist or antagonist (depending on the specific biochemical environment) by binding to the BMP4/Chordin complex. Recombinant human TSG is a 199 amino acid 22.2 kDa protein containing the BMP/TGFβ binding portion of the full length TSG protein.
Description: Twisted Gastrulation Protein (TSG) is a secreted BMP binding protein structurally related to the BMP antagonists Chordin and Noggin. TSG can inhibit BMP activity by binding directly to BMP proteins, and can act either as a BMP4 agonist or antagonist (depending on the specific biochemical environment) by binding to the BMP4/Chordin complex. Recombinant human TSG is a 199 amino acid 22.2 kDa protein containing the BMP/TGFβ binding portion of the full length TSG protein.
Description: Noggin belongs to a group of diffusible proteins which bind to ligands of the TGF-β family and regulate their activity by inhibiting their access to signaling receptors. The interplay between TGF-β ligands and their natural antagonists has major biological significance during development processes, in which cellular response can vary considerably depending upon the local concentration of the signaling molecule. Noggin was originally identified as a BMP-4 antagonist whose action is critical for proper formation of the head and other dorsal structures. Consequently, Noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of Noggin in mice results in prenatal death and recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing Noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant human Noggin is a 46 kDa disulfide-linked homodimer (120-10C) consisting of two 206 amino acid polypeptide chains. Monomeric glycosylated Noggin migrates at an apparent molecular weight of approximately 28.0-33.0 kDa by SDS PAGE analysis under reducing conditions.
Description: Noggin belongs to a group of diffusible proteins which bind to ligands of the TGF-β family and regulate their activity by inhibiting their access to signaling receptors. The interplay between TGF-β ligands and their natural antagonists has major biological significance during development processes, in which cellular response can vary considerably depending upon the local concentration of the signaling molecule. Noggin was originally identified as a BMP-4 antagonist whose action is critical for proper formation of the head and other dorsal structures. Consequently, Noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of Noggin in mice results in prenatal death and recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing Noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant human Noggin is a 46 kDa disulfide-linked homodimer (120-10C) consisting of two 206 amino acid polypeptide chains. Monomeric glycosylated Noggin migrates at an apparent molecular weight of approximately 28.0-33.0 kDa by SDS PAGE analysis under reducing conditions.
Description: Follistatin is a secreted protein that binds to ligands of the TGF-β family and regulates their activity by inhibiting their access to signaling receptors. It was originally discovered as activin antagonists whose activity suppresses expression and secretion of the pituitary hormone FSH (follicle stimulating hormone). In addition to being a natural antagonist, follistatin can inhibit the activity of other TGF-β ligands including BMP-2,-4,-6,-7, Myostatin, GDF-11, and TGF-β1. Follistatin is expressed in the pituitary, ovaries, decidual cells of the endometrium, and in some other tissues. Recombinant human Follistatin is a 31.5 kDa protein containing 288 amino acids. Its primary structure contains three cysteine-rich domains (called FS domains), each followed by a protease-inhibitory kazal domain.
Description: Follistatin is a secreted protein that binds to ligands of the TGF-β family and regulates their activity by inhibiting their access to signaling receptors. It was originally discovered as activin antagonists whose activity suppresses expression and secretion of the pituitary hormone FSH (follicle stimulating hormone). In addition to being a natural antagonist, follistatin can inhibit the activity of other TGF-β ligands including BMP-2,-4,-6,-7, Myostatin, GDF-11, and TGF-β1. Follistatin is expressed in the pituitary, ovaries, decidual cells of the endometrium, and in some other tissues. Recombinant human Follistatin is a 31.5 kDa protein containing 288 amino acids. Its primary structure contains three cysteine-rich domains (called FS domains), each followed by a protease-inhibitory kazal domain.
Description: CTGFL/WISP-2 is a 24.3 kDa protein that belongs to the CCN family of cysteine rich regulatory proteins. Members of this family stimulate mitosis, adhesion, apoptosis, extracellular matrix production, growth arrest, and migration of multiple cell types. The protein is expressed in primary osteoblasts, fibroblasts, ovary, testes, and heart. In addition to promoting adhesion of osteoblasts, CTGFL/WISP-2 inhibits osteocalcin production, as well as binding of fibrinogen to integrin receptors. Recombinant human CTGFL/WISP-2 is a 24.3 kDa protein of 228 amino acid residues.
Description: CTGFL/WISP-2 is a 24.3 kDa protein that belongs to the CCN family of cysteine rich regulatory proteins. Members of this family stimulate mitosis, adhesion, apoptosis, extracellular matrix production, growth arrest, and migration of multiple cell types. The protein is expressed in primary osteoblasts, fibroblasts, ovary, testes, and heart. In addition to promoting adhesion of osteoblasts, CTGFL/WISP-2 inhibits osteocalcin production, as well as binding of fibrinogen to integrin receptors. Recombinant human CTGFL/WISP-2 is a 24.3 kDa protein of 228 amino acid residues.
Description: CTGF is a member of the CCN family of secreted cysteine rich regulatory proteins and is the major mitogenic and chemoattractant protein produced by umbilical vein and vascular endothelial cells. CTGF stimulates the proliferation and differentiation of chondrocytes, induces angiogenesis, promotes cell adhesion of fibroblasts, endothelial, and epithelial cells, and binds to IGF, TGF beta1, and BMP-4. Cell migration and adhesion are signaled through binding to specific cell surface integrins and to heparin sulfate proteoglycans CTGF (98 a.a.), a lower molecular weight isoform containing the C-terminal portion of the full length CTGF protein, exerts full heparin binding, cell adhesion, and mitogenic CTGF activity. Recombinant human CTGF is a 11.2 kDa protein of 98 amino acid residues.
Description: CTGF is a member of the CCN family of secreted cysteine rich regulatory proteins and is the major mitogenic and chemoattractant protein produced by umbilical vein and vascular endothelial cells. CTGF stimulates the proliferation and differentiation of chondrocytes, induces angiogenesis, promotes cell adhesion of fibroblasts, endothelial, and epithelial cells, and binds to IGF, TGF beta1, and BMP-4. Cell migration and adhesion are signaled through binding to specific cell surface integrins and to heparin sulfate proteoglycans CTGF (98 a.a.), a lower molecular weight isoform containing the C-terminal portion of the full length CTGF protein, exerts full heparin binding, cell adhesion, and mitogenic CTGF activity. Recombinant human CTGF is a 11.2 kDa protein of 98 amino acid residues.
Description: CYR61 is a member of the CCN family of secreted cysteine rich regulatory proteins. CYR61 induces angiogenesis by stimulating the proliferation, migration, and adhesion of endothelial cells. Cell migration and adhesion are mediated through binding to specific cell surface integrins and to heparin sulfate proteoglycans. Increased expression of CYR61 is associated with several types of cancer, and correlates with the progression and estrogen independence of human breast cancers. Recombinant human CYR61 is a 39.5 kDa protein containing 357 amino acid residues. It is composed of four distinct structural domains (modules); the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the Thrombospondin type-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).
Description: CYR61 is a member of the CCN family of secreted cysteine rich regulatory proteins. CYR61 induces angiogenesis by stimulating the proliferation, migration, and adhesion of endothelial cells. Cell migration and adhesion are mediated through binding to specific cell surface integrins and to heparin sulfate proteoglycans. Increased expression of CYR61 is associated with several types of cancer, and correlates with the progression and estrogen independence of human breast cancers. Recombinant human CYR61 is a 39.5 kDa protein containing 357 amino acid residues. It is composed of four distinct structural domains (modules); the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the Thrombospondin type-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).
Description: NOV is a member of the CCN family of secreted cysteine rich regulatory proteins. The full length NOV protein contains four structural domains that confer distinct, and sometimes opposing, biological activities. Elevated expression of NOV is associated with certain tumors, including Wilm’s tumor and most nephroblastomas. However, in other tumor types and certain cancer cell lines, increased tumorgenicity and proliferation is correlated with decreased NOV expression. Additionally, NOV induces cell adhesion and cell migration by signaling through specific cell surface integrins and by binding to heparin sulfate proteoglycans and to fibulin 1C. NOV has also been reported to exert proangiogenic activities. Recombinant human NOV is a 36.2 kDa protein containing 331 amino acid residues. It is composed of four distinct structural domains (modules); the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the Thrombospondin type-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).
Description: NOV is a member of the CCN family of secreted cysteine rich regulatory proteins. The full length NOV protein contains four structural domains that confer distinct, and sometimes opposing, biological activities. Elevated expression of NOV is associated with certain tumors, including Wilm’s tumor and most nephroblastomas. However, in other tumor types and certain cancer cell lines, increased tumorgenicity and proliferation is correlated with decreased NOV expression. Additionally, NOV induces cell adhesion and cell migration by signaling through specific cell surface integrins and by binding to heparin sulfate proteoglycans and to fibulin 1C. NOV has also been reported to exert proangiogenic activities. Recombinant human NOV is a 36.2 kDa protein containing 331 amino acid residues. It is composed of four distinct structural domains (modules); the IGF binding protein (IGFBP) domain, the von Willebrand Factor C (VWFC) domain, the Thrombospondin type-I (TSP type-1) domain, and a C-terminal cysteine knot-like domain (CTCK).
Description: MIA is the first discovered member of a family of secreted cytokines termed the MIA/OTOR family. The four known members of this family; MIA, MIA2, OTOR and TANGO each contain a Src homology-3 (SH3)-like domain. MIA is an autocrine growth regulatory protein secreted from chondrocytes and malignant melanoma cells that promotes melanoma metastasis by binding competitively to fibronectin and laminin in a manner that results in melanoma cell detachment from the extracellular matrix in vivo. Elevated levels of MIA may represent a clinically useful marker for diagnosis of melanoma metastasis as well as a potential marker for rheumatoid arthritis. Recombinant human MIA is a 12.2 kDa globular protein containing 108 amino acid residues including two intramolecular disulfide bonds.
Description: MIA is the first discovered member of a family of secreted cytokines termed the MIA/OTOR family. The four known members of this family; MIA, MIA2, OTOR and TANGO each contain a Src homology-3 (SH3)-like domain. MIA is an autocrine growth regulatory protein secreted from chondrocytes and malignant melanoma cells that promotes melanoma metastasis by binding competitively to fibronectin and laminin in a manner that results in melanoma cell detachment from the extracellular matrix in vivo. Elevated levels of MIA may represent a clinically useful marker for diagnosis of melanoma metastasis as well as a potential marker for rheumatoid arthritis. Recombinant human MIA is a 12.2 kDa globular protein containing 108 amino acid residues including two intramolecular disulfide bonds.
Description: OTOR, also called Otoraplin and MIAL, is a secreted cytokine and a member of the MIA/OTOR family. Members of this family which also includes MIA, MIA2, and TANGO share a Src homology-3 (SH3)-like domain. OTOR is predominantly expressed in the cochlea of the inner-ear and to a lesser extent in fetal brain and in some cartilage tissues. OTOR appears to be involved in early chondrogenesis of the otic capsule, which is required for normal inner ear development and auditory function. Recombinant human OTOR is a 12.7 kDa globular protein containing 112 amino acid residues.
Description: OTOR, also called Otoraplin and MIAL, is a secreted cytokine and a member of the MIA/OTOR family. Members of this family which also includes MIA, MIA2, and TANGO share a Src homology-3 (SH3)-like domain. OTOR is predominantly expressed in the cochlea of the inner-ear and to a lesser extent in fetal brain and in some cartilage tissues. OTOR appears to be involved in early chondrogenesis of the otic capsule, which is required for normal inner ear development and auditory function. Recombinant human OTOR is a 12.7 kDa globular protein containing 112 amino acid residues.
Description: Vaspin is a newly described adipocytokine expressed predominantly in visceral white adipose tissues. Structure analysis of Vaspin predicts the presence of three β-sheets, nine α-helices, and one central loop, which are distinctive structural features of Serpin family members. The serpins are irreversible ("suicidal”) serine-protease inhibitors, characterized by having more than 30% sequence homology with α1-antitrypsin and a conserved tertiary structure, which contains an exposed reactive center loop that acts as a pseudo-substrate for the target proteinase. Members of this family play an important role in a number of fundamental biological processes including blood coagulation, fibrinolysis, complement activation, angiogenesis, inflammation, and tumor suppression. In human, the serpins represent approximately 2% of total serum proteins, of which 70% is α1- antitrypsin. Vaspin exhibits 40.2% sequence identity with α-1-antitrypsin. Yet, its protease inhibitory activity is still unknown. Vaspin mRNA expression in visceral fat is positively correlated with BMI and percent of body fat. Administration of Vaspin to obese mice improved glucose tolerance and insulin sensitivity, reflected by normalized blood glucose levels. It also led to the reversal of altered expression of diabetes-relevant adipocytokines including leptin, adiponectin, resistin, and TNF-α. These findings suggest a potential clinical use for Vaspin in ameliorating certain aberrations seen in the diabetic/obesity metabolic syndrome. Recombinant human Vaspin is a 45.2 kDa protein containing 395 amino-acid residues.
Description: Vaspin is a newly described adipocytokine expressed predominantly in visceral white adipose tissues. Structure analysis of Vaspin predicts the presence of three β-sheets, nine α-helices, and one central loop, which are distinctive structural features of Serpin family members. The serpins are irreversible ("suicidal”) serine-protease inhibitors, characterized by having more than 30% sequence homology with α1-antitrypsin and a conserved tertiary structure, which contains an exposed reactive center loop that acts as a pseudo-substrate for the target proteinase. Members of this family play an important role in a number of fundamental biological processes including blood coagulation, fibrinolysis, complement activation, angiogenesis, inflammation, and tumor suppression. In human, the serpins represent approximately 2% of total serum proteins, of which 70% is α1- antitrypsin. Vaspin exhibits 40.2% sequence identity with α-1-antitrypsin. Yet, its protease inhibitory activity is still unknown. Vaspin mRNA expression in visceral fat is positively correlated with BMI and percent of body fat. Administration of Vaspin to obese mice improved glucose tolerance and insulin sensitivity, reflected by normalized blood glucose levels. It also led to the reversal of altered expression of diabetes-relevant adipocytokines including leptin, adiponectin, resistin, and TNF-α. These findings suggest a potential clinical use for Vaspin in ameliorating certain aberrations seen in the diabetic/obesity metabolic syndrome. Recombinant human Vaspin is a 45.2 kDa protein containing 395 amino-acid residues.
Description: Maspin (mammary serine protease inhibitor) is a non-inhibitory serpin that is expressed predominantly in normal mammary epithelial cells but at significantly reduced levels or absent in most breast carcinomas. It has the ability to block the growth, invasiveness, and metastatic potential of breast and lung tumors. This anti-tumor activity is achieved, in part, by the ability of Maspin to inhibit angiogenesis and to preferentially promote apoptosis of tumor cells. Recombinant human Maspin is a 42.2 kDa non-glycosylated protein containing 375 amino acid residues.
Description: Maspin (mammary serine protease inhibitor) is a non-inhibitory serpin that is expressed predominantly in normal mammary epithelial cells but at significantly reduced levels or absent in most breast carcinomas. It has the ability to block the growth, invasiveness, and metastatic potential of breast and lung tumors. This anti-tumor activity is achieved, in part, by the ability of Maspin to inhibit angiogenesis and to preferentially promote apoptosis of tumor cells. Recombinant human Maspin is a 42.2 kDa non-glycosylated protein containing 375 amino acid residues.
Description: PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is a 50 kDa glycoprotein produced and secreted in many tissues throughout the body. A major component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. In addition, PEDF is able to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuroprotective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recent identification of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity (1) should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities implicate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF also has the potential to be useful in the treatment of various angiogenesis-related diseases including a number of cancers. Recombinant PEDF is a 44.5 kDa non-glycosylated protein containing 400 amino acid residues. (1) Notari, I. et al. J Biol Chem., Vol. 281, 38022-38037.
Description: PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is a 50 kDa glycoprotein produced and secreted in many tissues throughout the body. A major component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. In addition, PEDF is able to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuroprotective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recent identification of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity (1) should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities implicate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF also has the potential to be useful in the treatment of various angiogenesis-related diseases including a number of cancers. Recombinant PEDF is a 44.5 kDa non-glycosylated protein containing 400 amino acid residues. (1) Notari, I. et al. J Biol Chem., Vol. 281, 38022-38037.
Description: CD34 is a highly glycosylated type I membrane protein that is selectively expressed on hematopoietic stem cells and vascular endothelium. It has been widely used as a molecular marker for the identification, isolation, and manipulation of hemopoietic stem cells and progenitors. CD34 can function as a regulator of hemopoietic cell adhesion by mediating the attachment of stem cells to bone marrow stromal cells or other bone marrow components. The full length human CD34 is a 385 amino acid protein, consisting of a 31 amino acid signal sequence, a 74 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain and a 259 amino acid extracellular domain. Recombinant human sCD34 is a 258 amino acid polypeptide containing only the extracellular domain of the full length CD34 protein.
Description: CD34 is a highly glycosylated type I membrane protein that is selectively expressed on hematopoietic stem cells and vascular endothelium. It has been widely used as a molecular marker for the identification, isolation, and manipulation of hemopoietic stem cells and progenitors. CD34 can function as a regulator of hemopoietic cell adhesion by mediating the attachment of stem cells to bone marrow stromal cells or other bone marrow components. The full length human CD34 is a 385 amino acid protein, consisting of a 31 amino acid signal sequence, a 74 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain and a 259 amino acid extracellular domain. Recombinant human sCD34 is a 258 amino acid polypeptide containing only the extracellular domain of the full length CD34 protein.
Description: SPARC/Osteonectin is a secreted, evolutionarily conserved collagen-binding glycoprotein that is involved in a variety of cellular activities. It is highly expressed in tissues undergoing morphogenesis, remodeling and wound repair. SPARC/Osteonectin and its related peptides bind to numerous proteins of the extracellular matrix (ECM), affect ECM protein expression, influence cellular adhesion and migration, and modulate growth factor-induced cell proliferation and angiogenesis. SPARC/Osteonectin consists of three domains; an N-terminal acidic region that binds calcium ions with low affinity, a module containing two EF-hand motifs that bind calcium with high affinity, and a cysteine-rich follistatin-like domain. Recombinant human SPARC/Osteonectin is a glycoprotein containing 286 amino acids that migrates at an apparent MW of 43.7 kDa by SDS-PAGE analysis due to the effect of glycosylation.
Description: SPARC/Osteonectin is a secreted, evolutionarily conserved collagen-binding glycoprotein that is involved in a variety of cellular activities. It is highly expressed in tissues undergoing morphogenesis, remodeling and wound repair. SPARC/Osteonectin and its related peptides bind to numerous proteins of the extracellular matrix (ECM), affect ECM protein expression, influence cellular adhesion and migration, and modulate growth factor-induced cell proliferation and angiogenesis. SPARC/Osteonectin consists of three domains; an N-terminal acidic region that binds calcium ions with low affinity, a module containing two EF-hand motifs that bind calcium with high affinity, and a cysteine-rich follistatin-like domain. Recombinant human SPARC/Osteonectin is a glycoprotein containing 286 amino acids that migrates at an apparent MW of 43.7 kDa by SDS-PAGE analysis due to the effect of glycosylation.
Description: Betacellulin is an EGF-related polypeptide growth factor that signals through the EGF receptor. It is produced in several tissues, including the pancreas, small intestine, and in certain tumor cells. Betacellulin is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. Betacellulin is initially synthesized as a glycosylated 32.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce the mature sequence. Recombinant murine Betacellulin is a 9.0 kDa monomeric protein, containing 80 amino residues, which comprises the mature EGF homologous portion of the Betacellulin protein.
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