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: 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. 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: 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: 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: 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: 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: Protein CutA (CUTA) posseses a signal peptide and is widely expressed in brain. CUTA mayforms part of a complex of membrane proteins attached to acetylcholinesterase (AChE). CUTA takes part in cellular tolerance to a broad range of divalent cations other than copper. Alternate transcriptional splice variants, both protein-coding and non-protein-coding, have been found.
TAGLN Recombinant Protein (Rat) (Recombinant- Tag)
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.
TAGLN2 Recombinant Protein (Rat) (Recombinant Tag)
Description: All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. The GRO proteins chemoattract and activate neutrophils and basophils. Recombinant murine KC is a 7.8 kDa protein consisting of 72 amino acids including the 'ELR' motif common to the CXC chemokine family that bind to CXCR1 or CXCR2.
Description: All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. The GRO proteins chemoattract and activate neutrophils and basophils. Recombinant murine KC is a 7.8 kDa protein consisting of 72 amino acids including the 'ELR' motif common to the CXC chemokine family that bind to CXCR1 or CXCR2.
Description: Tissue Factor (TF) is a single-pass type I membrane glycoprotein member of the tissue factor family. TF expression is highly dependent upon cell type. This factor enables cells to initiate the blood coagulation cascades, and it functions as the high-affinity receptor for the coagulation factor VII. TF initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The complex activates factors IX or X by specific limited protolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade.
Description: T-cell antigen CD7 (CD7) is also known as GP40, LEU-9, TP41 and Tp40. CD7 is a protein that in humans is encoded by the CD7 gene, this gene encodes a transmembrane protein which is a member of the immunoglobulin superfamily. CD7 has been shown to interact with PIK3R1. This protein is found on thymocytes and mature T cells. It plays an essential role in T-cell interactions and also in T-cell/B-cell interaction during early lymphoid development.
Description: AXL Receptor Tyrosine Kinase is also known as Tyrosine-protein kinase receptor UFO, which belongs to the protein kinase superfamily, Tyr protein kinase family and AXL/UFO subfamily. AXL contains two fibronectin type-III domains, two Ig-like C2-type (immunoglobulin-like) domains and one protein kinase domain. AXL is highly expressed in metastatic colon tumors. AXL is activated by GAS6-binding and subsequent autophosphorylation. AXL is involved in signal transduction from the extracellular matrix into the cytoplasm by binding growth factors, and thus implicated in the stimulation of cell proliferation.
Description: Hepatocyte growth factor (HGF) is a paracrine cellular growth, motility and morphogenic factor. Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization. Hepatocyte growth factor is secreted by mesenchymal cells and acts as a multi-functional cytokine on cells of mainly epithelial origin. Its ability to stimulate mitogenesis, cell motility, and matrix invasion gives it a central role in angiogenesis, tumorogenesis, and tissue regeneration. In addition, HGF has been implicated in a variety of cancers, including of the lungs, pancreas, thyroid, colon, and breast.
Description: Human epidermal growth factor (EGF) is also known as HOMG4 and URG,and is a growth factor that plays an important role in the regulation of cell growth, proliferation, and differentiation by binding to its receptor EGFR. Epidermal growth factor can be found in human platelets, macrophages, urine, saliva, milk, and plasma. EGF is the founding member of the EGF-family of proteins. Members of this protein family have highly similar structural and functional characteristics. All family members contain one or more repeats of the conserved amino acid sequence. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents. Because of the increased risk of cancer by EGF, inhibiting it decreases cancer risk.
Description: Human epidermal growth factor (EGF) is also known as HOMG4 and URG,and is a growth factor that plays an important role in the regulation of cell growth, proliferation, and differentiation by binding to its receptor EGFR. Epidermal growth factor can be found in human platelets, macrophages, urine, saliva, milk, and plasma. EGF is the founding member of the EGF-family of proteins. Members of this protein family have highly similar structural and functional characteristics. All family members contain one or more repeats of the conserved amino acid sequence. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents. Because of the increased risk of cancer by EGF, inhibiting it decreases cancer risk.
Description: Protein p62 preferentially binds multiubiquitin chains and forms a novel cytoplasmic structure "sequestosome" which serves as a storage place for ubiquitinated proteins.
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: 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: 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: 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: Stem Cell Factor (SCF) is a hematopoietic growth factor that exerts its activity by signaling through the c-Kit receptor. SCF and c-Kit are essential for the survival, proliferation and differentiation of hematopoietic cells committed to the melanocyte and germ cell lineages. Human SCF manifests low activity on murine cells, while murine and rat SCF are fully active on human cells. Recombinant human SCF is an 18.4 kDa polypeptide containing 165 amino acid residues, which corresponds to the sequence of the secreted soluble form of SCF.
Description: Stem Cell Factor (SCF) is a hematopoietic growth factor that exerts its activity by signaling through the c-Kit receptor. SCF and c-Kit are essential for the survival, proliferation and differentiation of hematopoietic cells committed to the melanocyte and germ cell lineages. Human SCF manifests low activity on murine cells, while murine and rat SCF are fully active on human cells. Recombinant human SCF is an 18.4 kDa polypeptide containing 165 amino acid residues, which corresponds to the sequence of the secreted soluble form of SCF.
Description: Murine C10 belongs to the CC chemokine family and is expressed in myelopoietic bone marrow cultures when stimulated with GM-CSF, M-CSF, IL-3 or IL-4. It signals primarily through the CCR1 receptor. C10 is chemotactic for B cells, CD4+ T cells, monocytes and NK cells and also exhibits powerful suppressive activity on colony formation by different lineages of hematopoietic progenitors. The C10 contains the four highly conserved cysteine residues present in CC chemokines. The mature protein contains 95 amino acid residues. Recombinant murine C-10 is a 10.7 kDa protein containing 95 amino acid residues.
Description: Murine C10 belongs to the CC chemokine family and is expressed in myelopoietic bone marrow cultures when stimulated with GM-CSF, M-CSF, IL-3 or IL-4. It signals primarily through the CCR1 receptor. C10 is chemotactic for B cells, CD4+ T cells, monocytes and NK cells and also exhibits powerful suppressive activity on colony formation by different lineages of hematopoietic progenitors. The C10 contains the four highly conserved cysteine residues present in CC chemokines. The mature protein contains 95 amino acid residues. Recombinant murine C-10 is a 10.7 kDa protein containing 95 amino acid residues.
Description: CXCL6, also known as GCP-2 in humans and LIX in mice, is a connective tissue-derived CXC chemokine that contains the four conserved cysteine residues shared by CXC chemokines and the ‘ELR’ motif responsible for CXCR1 and CXCR2 receptor signaling. Constitutively expressed in monocytes, platelets, endothelial cells and mast cells, CXCL6 selectively chemoattracts neutrophils and has been shown to exert anti-angiogenic activity. Human GCP-2 and murine LIX respectively exhibit murine and human cell cross-reactivity. There are two naturally occurring variants of murine LIX, the 78 amino-acid-length LIX 1-78 (GCP-2) and the 70 amino-acid-length LIX 9-78 (GCP-2).
Description: CXCL6, also known as GCP-2 in humans and LIX in mice, is a connective tissue-derived CXC chemokine that contains the four conserved cysteine residues shared by CXC chemokines and the ‘ELR’ motif responsible for CXCR1 and CXCR2 receptor signaling. Constitutively expressed in monocytes, platelets, endothelial cells and mast cells, CXCL6 selectively chemoattracts neutrophils and has been shown to exert anti-angiogenic activity. Human GCP-2 and murine LIX respectively exhibit murine and human cell cross-reactivity. There are two naturally occurring variants of murine LIX, the 78 amino-acid-length LIX 1-78 (GCP-2) and the 70 amino-acid-length LIX 9-78 (GCP-2).
Description: MIG, a CXC chemokine, is produced by IFN?× stimulated monocytes, macrophages and endothelial cells. It signals through the CXCR3 receptor. MIG selectively chemoattracts Th1 lymphocytes, and also exerts other activities including inhibition of tumor growth, angiogenesis, and inhibition of colony formation of hematopoietic progenitors. Human MIG is active on murine cells. Recombinant murine MIG is a 12.2 kDa protein containing 105 amino acid residues, including the four highly conserved cysteine residues present in CXC chemokines.
Description: MIG, a CXC chemokine, is produced by IFN?× stimulated monocytes, macrophages and endothelial cells. It signals through the CXCR3 receptor. MIG selectively chemoattracts Th1 lymphocytes, and also exerts other activities including inhibition of tumor growth, angiogenesis, and inhibition of colony formation of hematopoietic progenitors. Human MIG is active on murine cells. Recombinant murine MIG is a 12.2 kDa protein containing 105 amino acid residues, including the four highly conserved cysteine residues present in CXC chemokines.
Description: MDC is a CC chemokine that is produced in B cells, macrophages, monocyte-derived dendritic cells, activated NK cells and CD4 T cells. It signals through the CCR4 receptor. MDC chemoattracts monocytes, dendritic cells and NK cells and exerts HIV suppressive activity. The 67 amino acid form of MDC displays reduced chemoattractant activity but retains HIV suppressive activity. Recombinant murine MDC is a 7.8 kDa protein containing 68 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Description: MDC is a CC chemokine that is produced in B cells, macrophages, monocyte-derived dendritic cells, activated NK cells and CD4 T cells. It signals through the CCR4 receptor. MDC chemoattracts monocytes, dendritic cells and NK cells and exerts HIV suppressive activity. The 67 amino acid form of MDC displays reduced chemoattractant activity but retains HIV suppressive activity. Recombinant murine MDC is a 7.8 kDa protein containing 68 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Description: BCA-1/BLC, a CXC chemokine, is expressed in the liver, spleen, lymph nodes, appendix and stomach. It exerts its activities through its only receptor CXCR5. BCA-1/BLC is a potent chemoattractant for B lymphocytes and induces weak chemotactic response in T cells and macrophages. It manifests no activity on neutrophils and monocytes. Recombinant murine BLC is a 9.8 kDa protein containing 88 amino acid residues including the four highly conserved cysteine residues present in CXC chemokines.
Description: BCA-1/BLC, a CXC chemokine, is expressed in the liver, spleen, lymph nodes, appendix and stomach. It exerts its activities through its only receptor CXCR5. BCA-1/BLC is a potent chemoattractant for B lymphocytes and induces weak chemotactic response in T cells and macrophages. It manifests no activity on neutrophils and monocytes. Recombinant murine BLC is a 9.8 kDa protein containing 88 amino acid residues including the four highly conserved cysteine residues present in CXC chemokines.
Description: MEC is a secreted CC chemokine expressed primarily by epithelial cells of the bronchioles, salivary gland, mammary gland and colon. MEC signals through the CCR10 receptor and chemoattracts resting CD4, CD8 T-cells and eosinophils. MEC contains six cysteines including the four highly conserved cysteine residues present in CC chemokines. Recombinant murine MEC is a 12.6 kDa protein containing 111 amino acid residues.
Description: MEC is a secreted CC chemokine expressed primarily by epithelial cells of the bronchioles, salivary gland, mammary gland and colon. MEC signals through the CCR10 receptor and chemoattracts resting CD4, CD8 T-cells and eosinophils. MEC contains six cysteines including the four highly conserved cysteine residues present in CC chemokines. Recombinant murine MEC is a 12.6 kDa protein containing 111 amino acid residues.
Description: CXCL6, also known as GCP-2 in humans and LIX in mice, is a connective tissue-derived CXC chemokine that contains the four conserved cysteine residues shared by CXC chemokines and the ‘ELR’ motif responsible for CXCR1 and CXCR2 receptor signaling. Constitutively expressed in monocytes, platelets, endothelial cells and mast cells, CXCL6 selectively chemoattracts neutrophils and has been shown to exert anti-angiogenic activity. Human GCP-2 and murine LIX respectively exhibit murine and human cell cross-reactivity. There are two naturally occurring variants of murine LIX, the 78 amino-acid-length LIX 1-78 (GCP-2) and the 70 amino-acid-length LIX 9-78 (GCP-2).
Description: CXCL6, also known as GCP-2 in humans and LIX in mice, is a connective tissue-derived CXC chemokine that contains the four conserved cysteine residues shared by CXC chemokines and the ‘ELR’ motif responsible for CXCR1 and CXCR2 receptor signaling. Constitutively expressed in monocytes, platelets, endothelial cells and mast cells, CXCL6 selectively chemoattracts neutrophils and has been shown to exert anti-angiogenic activity. Human GCP-2 and murine LIX respectively exhibit murine and human cell cross-reactivity. There are two naturally occurring variants of murine LIX, the 78 amino-acid-length LIX 1-78 (GCP-2) and the 70 amino-acid-length LIX 9-78 (GCP-2).
Description: MIG, a CXC chemokine, is produced by IFN stimulated monocytes, macrophages and endothelial cells. It signals through the CXCR3 receptor. MIG selectively chemoattracts Th1 lymphocytes, and also exerts other activities including inhibition of tumor growth, angiogenesis, and inhibition of colony formation of hematopoietic progenitors. Human MIG is active on murine cells. Recombinant human MIG is an 11.7 kDa protein containing 103 amino acid residues, including the four highly conserved cysteine residues present in CXC chemokines.
Description: MIG, a CXC chemokine, is produced by IFN stimulated monocytes, macrophages and endothelial cells. It signals through the CXCR3 receptor. MIG selectively chemoattracts Th1 lymphocytes, and also exerts other activities including inhibition of tumor growth, angiogenesis, and inhibition of colony formation of hematopoietic progenitors. Human MIG is active on murine cells. Recombinant human MIG is an 11.7 kDa protein containing 103 amino acid residues, including the four highly conserved cysteine residues present in CXC chemokines.
Description: MDC is a CC chemokine that is produced in B cells, macrophages, monocyte-derived dendritic cells, activated NK cells and CD4 T cells. It signals through the CCR4 receptor. MDC chemoattracts monocytes, dendritic cells and NK cells and exerts HIV suppressive activity. The 67 amino acid form of MDC displays reduced chemoattractant activity but retains HIV suppressive activity. Recombinant human MDC is an 8.0 kDa protein containing 67 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Description: MDC is a CC chemokine that is produced in B cells, macrophages, monocyte-derived dendritic cells, activated NK cells and CD4 T cells. It signals through the CCR4 receptor. MDC chemoattracts monocytes, dendritic cells and NK cells and exerts HIV suppressive activity. The 67 amino acid form of MDC displays reduced chemoattractant activity but retains HIV suppressive activity. Recombinant human MDC is an 8.0 kDa protein containing 67 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Description: MDC is a CC chemokine that is produced in B cells, macrophages, monocyte-derived dendritic cells, activated NK cells and CD4 T cells. It signals through the CCR4 receptor. MDC chemoattracts monocytes, dendritic cells and NK cells and exerts HIV suppressive activity. The 67 amino acid form of MDC displays reduced chemoattractant activity but retains HIV suppressive activity. Recombinant human MDC is an 8.1 kDa protein containing 69 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.
Ronald
