6348 Results for: "Peprotech"

Supplier: Peprotech

IL-17D is a disulfide-linked homodimer of two 185 amino acid polypeptide chains. It belongs to the IL-17 family of structurally-related cytokines that share a highly conserved C-terminal region, but differ from one another in their N-terminal regions and in their distinct biological roles. The six known members of this family, IL-17A through IL-17F, are secreted as homodimers. IL-17D has the ability to stimulate the production of IL-6, IL-8 and GM-CSF, and inhibits hemopoiesis of myeloid progenitor cells in colony-forming assays. Recombinant Human IL-17D is a 40.5 kDa disulfide-linked homodimer of two 185 amino acid polypeptide chains.

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IL-17E is a disulfide-linked homodimer of two 145 amino acid polypeptide chains. It belongs to the IL-17 family of structurally-related cytokines that share a highly conserved C-terminal region, but differ from one another in their N-terminal regions and in their distinct biological roles. The six known members of this family, IL-17A through IL-17F, are secreted as homodimers. IL-17E stimulates secretion of IL-8, and induces activation of the transcription factor NF-κB in cells that express the IL-17BR receptor. Recombinant Human IL-17E is a 33.8 kDa disulfide-linked homodimer of two 146 amino acid polypeptide chains.

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CXCL16 is a member of the CXC chemokine family and signals through the CXCR6 receptor. CXCL16 may play a role in attracting lymphocyte subsets during inflammation and may facilitate certain immune responses. The chemokine domain of CXCL16 contains six cysteine residues, including the four highly conserved cysteine residues characteristic of CXC chemokines. The CXCL16 gene codes for a 273 amino acid polypeptide, which includes a 29 amino acid cytoplasmic domain and transmembrane sequence containing approximately 20 amino acids. The extracellular portion of CXCL16 contains a chemokines domain and an extended C-terminal “mucin-like stalk” sequence. The extracellular domain contains 89 amino acid residues (86 a.a. residues for the murine homolog). Recombinant Human CXCL16 is a 10.1 kDa protein containing 89 amino acid residues.

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Serum amyloid A proteins (SAA) represents a family of apolipoproteins that circulates in association with high-density lipoproteins (HDL). The level of Apo-SAA, normally 1-5 μg/ml in plasma, increases 500-1000 fold within 24 hours of an inflammatory stimulus and, under these conditions, is the most abundant HDL apolipoprotein. The human SAA gene codes for a 122 amino acid nonglycosylated polypeptide, which contains an 18 amino acid N-terminal sequence. Recombinant Human Apo-SAA1 is an 11.7 kDa protein containing 105 amino acid residues.

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The Semphorins are a large family of phylogenetically conserved proteins that play a pivotal role in maintaining homeostasis in the immune system. Twenty members of this family have been identified and categorized into eight subclasses based on sequence similarity and distinctive structural features. CD100, also known as Sema4D, is a 150 kDa transmembrane class IV semaphorin. Studies have shown that CD100 can induce monocyte migration, T-cell activation, and B-cell survival, as well as T/B cell and T/DC “cooperation”. The CD100 precursor contains 862 amino acids, including a 21 a.a. signal sequence, a 713 a.a. extracellular domain, a 21 a.a. transmembrane sequence, and a 107 a.a. cytoplasmic region. The extracellular sequence contains several structural features, including a 479 a.a. “sema” domain, a 79 a.a. Ig-like sequence, and a 52 a.a. “Plexin-type repeat”. Recombinant Human sCD100 is a 78.9 kDa protein comprising the extracellular domain of CD100 (711 amino acids). SDS-PAGE analysis run under non-reducing conditions shows a mixture of disulfide linked dimer and monomer.

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SDF-1α and β are stromal-derived, CXC chemokines that signal through the CXCR4 receptor. SDF-1α and β chemoattract B and T cells, and have been shown to induce migration of CD34+ stem cells. Additionally, the SDF-1 proteins exert HIV-suppressive activity in cells expressing the CXCR4 receptor. Human and murine SDF-1 proteins act across species. SDF-1α and β contain the four highly conserved cysteine residues present in CXC chemokines. The mature SDF-1α protein is the result of alternative splicing of the SDF-1 gene and contains 68 amino acid residues. Recombinant Murine SDF-1α (CXCL12) is a 7.9 kDa protein containing 68 amino acid residues.

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Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to specific residues or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Furin is a calcium-dependent serine endoprotease that processes numerous proproteins of different secretory pathways into their mature forms by cleaving at the carboxyl side of the recognition sequence, R-Xaa-(K/R)-R, where Xaa can be any amino acid. Recombinant Human Furin is a 63.9 kDa protein, corresponding to residues 131 through 715 of the Furin precursor, plus a C-terminal His-tag.

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Viral MIP-2 (vMIP-2) is a chemokine analog encoded by the human herpes virus, and has been shown to have antagonist activity towards several chemokine receptors. Recombinant Viral MIP-2 is a 7.9 kDa protein consisting of 70 amino acids, including the four highly conserved cysteine residues present in CC chemokines.

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EG-VEGF is a secreted angiogenetic mitogen growth factor expressed in the steroidogenic glands, ovary, testis, adrenal gland, and placenta. EG-VEGF induces proliferation, migration, and fenestration (formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. The murine EG-VEGF gene codes for a 105 amino acid polypeptide containing an N-terminal signal sequence of 19 amino acids. Recombinant Murine EG-VEGF is a 9.6 kDa protein consisting of 86 amino acid residues, including ten cysteine residues that potentially form five pairs of intra-molecular disulfide bonds.

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ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solubilization 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 the liver and brain, and to some extent in almost every organ. ApoE is an important constituent of all plasma lipoproteins. Its 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. 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.

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Complement 5a (C5a) is an enzymatically generated glycoprotein belonging to the anaphylatoxin family of structurally and functionally related proteins. Generated upon the activation of the complement system, C5a, together with C4a, C3a, and the membrane attack complex (C5b-9), functions as a central player in host defense by inducing smooth muscle cell contraction, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes through cell degranulation. In addition to acting as a direct mediator of localized inflammatory response, C5a also initiates both the synthesis and release of IL-8 from monocytes and bronchial epithelial cells, stimulates the proliferation of neurons and hepatocytes, and functions as a potent chemoattractant. Where C5a deficiency, a rare defect of the complement pathway caused by the mutation of the C5a gene, is associated with susceptibility to severe infections, excessive C5a activation has been linked to liver fibrosis, sepsis, adult respiratory distress syndrome, rheumatoid arthritis, Alzheimer’s disease, and ischemic heart disease. Human C5a shares 60% and 54% sequence identity to mouse and rat C5a, respectively. The human C5 gene encodes a 1,676 amino acid glycoprotein that is comprised of a disulfide-linked C5 alpha and a C5 beta chain, the former of which contains the active, 74 amino acid C5a anaphylatoxin chain. Recombinant Human C5a is an 8.28 kDa glycoprotein containing the 74 amino acid residues of the C5a anaphylatoxin chain.

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RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic cell-membrane protein, which, by interacting with RANKL, augments the ability of dendritic. These dendritic cells then stimulate naïve T-cell proliferation, and promote the survival of RANK + T-cells. RANK is also expressed in a variety of tissues, including skeletal muscle, thymus, liver, colon, small intestine, and adrenal gland. The RANK/RANKL interaction is important in the regulation of osteoclastogenesis, and in dendritic cell-mediated T-cell immune responses. Impairments in RANK signaling have been implicated in the induction of expansile osteolysis and Paget's disease of bone (PDB2). Recombinant Human sRANK Receptor is a 19.3 kDa polypeptide containing the TNFR-homologous, cysteine-rich portion of the extracellular domain of RANK receptor (175 amino acid residues).

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IL-13 is an immunoregulatory cytokine produced primarily by activated Th2 cells, and also by mast cells and NK cells. Targeted deletion of IL-13 in mice resulted in impaired Th2 cell development and indicated an important role for IL-13 in the expulsion of gastrointestinal parasites. IL-13 exerts anti-inflammatory effects on monocytes and macrophages and it inhibits the expression of inflammatory cytokines such as IL-1β, TNF-α, IL-6 and IL-8. IL-13 has also been shown to enhance B cell proliferation and to induce isotype switching, resulting in increased production of IgE. Blocking of IL-13 activity inhibits the pathophysiology of asthma. Human and murine IL-13 are cross-species reactive. Recombinant Rat IL-13 is an 11.9 kDa protein consisting of 109 amino acid residues.

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IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP6, which specifically inhibits IGF-II actions, is produced by bone cells and is the major IGF-BP present in cerebrospinal fluid. IGF-BP6 has been shown to inhibit IGF-II-dependent cancers such as neuroblastoma, colon cancer and rhabdomyosarcoma. Recombinant Human IGF-BP6 has a calculated mass of 22.3 kDa and consists of 213 amino acid residues, including the IGF-BP domain and thyroglobulin type-I domain. Recombinant Human IGF-BP6 migrates at an apparent molecular weight of approximately 23.0-30.0 kDa by SDS-PAGE analysis under non-reducing conditions.

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ApoA-I is a 29.0 kDa protein produced in the liver and intestine, and secreted as the predominant constituent of nascent high density lipoprotein (HDL) particle. ApoA-I, which is found exclusively in HDL, has a unique ability to capture and solubilize free cholesterol. This ApoA-I ability enables HDL to remove excess peripheral cholesterol, and return it to the liver for recycling and excretion. This process, called reverse cholesterol transport, is thought to inhibit atherogenesis. For this reason, HDL is also known as the “good cholesterol.” The therapeutic potential of ApoA-I has been recently assessed in patients with acute coronary syndromes, using a recombinant form of a naturally occurring variant of ApoA-I (called ApoA-I Milano). The availability of recombinant normal ApoA-I should facilitate further investigation into the potential usefulness of ApoA-I in preventing atherosclerotic vascular diseases. Recombinant Human ApoA-I is a 28.2 kDa protein of 244 amino acid residues.

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Both MIP-1α and MIP-1β are structurally and functionally related CC chemokines. They participate in host response to invading bacterial, viral, parasite and fungal pathogens, by regulating the trafficking, and activation state, of selected subgroups of inflammatory cells (e.g. macrophages, lymphocytes and NK cells). While both MIP-1α and MIP-1β exert similar effects on monocytes, their effect on lymphocytes differ; with MIP-1α selectively attracting CD8+ lymphocytes, and MIP-1β selectively attracting CD4+ lymphocytes. Additionally, MIP-1α and MIP-1β have also been shown to be potent chemoattractants for B cells, eosinophils and dendritic cells. Both human and murine MIP-1α and MIP-1β are active on human and murine hematopoietic cells. Recombinant Rat MIP-1α (CCL3) is a 7.8 kDa protein containing 69 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.

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GM-CSF is a hematopoietic growth factor that stimulates the development of neutrophils and macrophages, and promotes the proliferation and development of early erythroid megakaryocytic and eosinophilic progenitor cells. It is produced in by endothelial cells, monocytes, fibroblasts and T lymphocytes. GM-CSF inhibits neutrophil migration and enhances the functional activity of the mature end-cells. The human and murine molecules are species-specific and exhibit no cross-species reactivity. Recombinant Rat GM-CSF is a 14.5 kDa globular protein consisting of 128 amino acid residues.

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Human FSTL1 Recombinant Protein, Purity: >95% by SDS and HPLC, Source: CHO cells, Biological Activity: By its binding ability in a functional ELISA, Synonyms: Follistatin-like protein 1, FSL1, Follistatin-related pro

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Human MPF Recombinant Protein, Purity: >95% by SDS and HPLC, Source: CHO cells, Migrates with an apparent molecular mass of approximately 32-33 kDa by SDS, Synonyms: Mesothelin, MSLN, SMRP, CAK1 antigen, Pre-pro-megaka

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Produced from sera of rabbits immunized with highly pure Recombinant Human BD-5. Anti­Human BD-5­specific antibody was purified by affinity chromatography and then biotinylated.

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Recombinant Human/Murine/Rat Irisin, Purity: Greater than 90% by SDS-PAGE, Source: CHO cells, Cross Reactivity: Human, Mouse, Rat, Synonyms: Fibronectin type III domain-containing protein 5, Fibronectin type III repeat-containing protein 2, Size: 10UG

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Recombinant HumansCD28 Fc, Purity: Greater than 95% by SDS-PAGE gel and HPLC analyses, Source: CHO cells, Determined by its ability to bind its principal binding partner (B7-1) in a functional ELISA, Synonyms: T-cell-specific surface glycoprotein CD28, Size: 1MG

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Recombinant Murine Leptin (AF), Purity: Greater than 98% by SDS-PAGE gel and HPLC analyses, Source: E.coli, Cross Reactivity: Hamster, Human, Significant effects on body weight, food consumption and plasma glucose levels, Synonyms: Obesity protein (OB), Size: 1MG

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Animal-Free Human IL-37 Recombinant Protein, Purity: >95%, Source: E.coli, Biological Activity: By its ability to bind Interleukin-18 Binding Protein isoform a (IL-18 BPa) in functional ELISA, Synonyms: In

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FGF-acidic is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-acidic is a non-glycosylated heparin binding growth factor that is expressed in the brain, kidney, retina, smooth muscle cells, bone matrix, osteoblasts, astrocytes and endothelial cells. FGF-acidic has the ability to signal through all the FGF receptors. Recombinant Murine FGF-acidic is a 15.9 kDa protein consisting of 141 amino acid residues.

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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 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 Murine VEGF

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Produced from sera of goats immunized with highly pure Recombinant Human Eotaxin (CCL11). Anti­Human Eotaxin (CCL11)­specific antibody was purified by affinity chromatography employing an immobilized Human Eotaxin matrix.

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APRIL, a member of the TNF superfamily, is expressed in monocytes, macrophages, certain transformed cell lines, certain cancers of the colon, and lymphoid tissues. APRIL, along with another TNF family member, BAFF, competes for two receptors, TACI and BCMA. APRIL has the ability to stimulate proliferation of various tumor cell lines, including Jurkat T cells and MCF-7 carcinoma cells. Like BAFF, APRIL also stimulates the proliferation of B and T cells. The human APRIL gene codes for at least four alternatively spliced transcriptional variants, which give rise to different isoforms of the APRIL precursor protein. All isoforms can be cleaved by the protease, furin, to release a soluble C-terminal fragment, which comprises the TNF-like receptor binding of the APRIL precursor. Recombinant Murine APRIL is a soluble 21.9 kDa protein, consisting of 192 amino acid residues.

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EGF is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through a receptor known as c-erbB, which is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). Recombinant Rat EGF is a 6.2 kDa globular protein containing 54 amino acid residues, including 3 intramolecular disulfide bonds.

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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, that helps maintain pluripotency and self renewal via a STAT3-independent pathway. Recombinant Human Nanog is a 34.7 kDa protein, which is synthesized as a 304 amino acid polypeptide lacking a signal sequence for secretion.