6346 Results for: "Peprotech"

Supplier: Peprotech

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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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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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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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-megakar

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Recombinant Murine BD-2, Purity: Greater than 98% by SDS-PAGE gel and HPLC analyses, Source: E.coli, expressed on some leukocytes and at epithelial surfaces, Synonyms: Beta-Defensin 2, DEFB2, DEFB4A, Skin-Antimicrobial Peptide 1, SAP1, Size: 5UG

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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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IL-12 is a potent regulator of cell-mediated immune responses and it induces IFN-gamma production by NK and T cells. It is produced by activated monocytes/macrophage cells, B lymphocytes and connective tissue-type mast cells. Among its biological activities, IL-12 promotes the growth and activity of activated NK, CD4+ and CD8+ cells, and induces the development of IFN-gamma-producing Th1 cells. PeproTech's Recombinant Human IL-12 p70, derived from HEK293 cells, is a heterodimeric glycoprotein consisting of disulfide-linked p35 and p40 subunits (503 total amino acid residues). The calculated molecular weight of Human IL-12 p70 is 57.2 kDa; however, due to glycosylation, it migrates at an apparent molecular weight of 65-70 kDa based on SDS-PAGE gel, under non-reducing conditions.

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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

Supplier: Peprotech

IP-10 is a CXC chemokine that signals through the CXCR3 receptor. IP-10 selectively chemoattracts Th1 lymphocytes and monocytes, and inhibits cytokine-stimulated hematopoietic progenitor cell proliferation. Additionally, it is angiostatic and mitogenic for vascular smooth muscle cells. Recombinant Human IP-10 is an 8.6 kDa protein consisting of 77 amino acids, including the four conserved cysteine residues present in CXC chemokines.

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GDNF is a disulfide-linked, homodimeric neurotrophic factor structurally related to Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. GDNF signals through a multicomponent receptor system, composed of a RET and one of the four GFRα (α1-α4) receptors. GDNF specifically promotes dopamine uptake and survival, and morphological differentiation of midbrain neurons. Using a Parkinson’s disease mouse model, GDNF has been shown to improve conditions such as bradykinesia, rigidity, and postural instability. The functional murine GDNF ligand is a disulfide-linked homodimer consisting of two 15.1 kDa polypeptide chains called monomers. Each monomer contains seven conserved cysteine residues, including Cys-101, which is used for inter-chain disulfide bridging, and others that are involved in the intramolecular ring formation known as the cysteine knot configuration. The calculated molecular weight of Recombinant Murine GDNF is 30.2 kDa.

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RELMβ (Resistin-like molecule β/FIZZ2) is a disulfide-linked, homodimeric protein expressed in the epithelium of the colon and small bowel. The biological functions of RELMβ, and its molecular targets, are not fully known, but it has been suggested that it plays a regulatory role during inflammation, and may also act to establish links among adipose tissue, the intestine and the liver. Interestingly, the molecular structure of RELMβ is highly homologous to that of the adipose-derived cytokines, resistin and RELMα. These proteins share a highly conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. Recombinant Murine RELMβ is an 18.0 kDa protein, consisting of two identical 83 amino acid polypeptide chains linked by a single disulfide bond.

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Human IL-8, Monoclonal Antibody, Source: Mouse, Preparation: purified from cell culture by Protein G affinity chromatography, Immunogen: E.coli derived Recombinant Human IL-8, Application: ELISA, Western Blot, 500UG

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Monoclonal AntibodyProduced in mice immunized with highly pure Recombinant β-NGF. Anti­β-NGF­specific antibody was purified from cell culture by Protein G affinity chromatography.

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RAT IL-10, Monoclonal Antibody, Source: Mouse, Preparation: purified from tissue culture by Protein A affinity chromatography, Immunogen: E.coli derived Recombinant Rat IL-10, Application: ELISA, Western Blot, 500UG

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IL-17F, a member of the IL-17 family of structurally related cytokines, has been shown to stimulate proliferation and activation of T-cells and PBMCs. IL-17F also regulates cartilage matrix turnover and inhibits angiogenesis. Recombinant Murine IL-17F is a 30.0 kDa, disulfide-linked homodimer consisting of two 134 amino acid residue chains.

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Murine SF-20 is a bone marrow stroma-derived growth factor. SF20 is expressed in bone marrow, spleen stroma cells, resting mononuclear cells, resting CD8+ and CD19+ cells, and activated CD8+ T cells, and has been shown to bind to the surface of cells expressing the receptor TSA-1 (Thymic shared Ag-1). Among its biological activities, SF20 stimulates the proliferation of FDCP2 cells (a mouse factor-dependent hemopoietic cell line) and mouse lymphoid cells. Recombinant Murine SF-20 is a 15.8 kDa protein containing 143 amino acid residues.

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Eotaxin-2 is a CC chemokine that signals through the CCR3 receptor. It is produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3, including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Additionally, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which also includes a C-terminal truncation, contains 78 amino acid residues (92 a.a. residues for the murine homolog, without C-terminal truncation). Eotaxin-2 contains the four conserved cysteine residues present in CC chemokines. Recombinant Human Eotaxin-2 (CCL24) is an 8.8 kDa protein containing 78 amino acid residues.

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MIP-4 is a CC chemokine that is expressed in lymph nodes, lungs, placenta and bone marrow. MIP-4’s primary receptor is unknown. MIP-4 chemoattracts lymphocytes, and has been shown to exert activity on both CD4+ and CD8+ T cells. Recombinant Human MIP-4 (CCL18) is a 7.8 kDa protein containing 68 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.

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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 Murine EGF is a 6.0 kDa globular protein containing 53 amino acid residues, including 3 intramolecular disulfide bonds. Manufactured using all Animal-Free reagents.

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Wnt-1 is a secreted protein that signals through the Frizzled family of cell surface receptors, and is required for normal embryonic development. Wnt-1 activation induces a complex signaling cascade that ultimately leads to the increased expression of over fifty genes. An important component of Wnt-1 signaling is the stabilization, and resulting accumulation, of the intracellular signaling protein, β-catenin. Wnt signaling induces and maintains the transformed phenotype, and, in certain embryonic cell lines, supports self-renewal in the absence of significant differentiation. Elevated levels of Wnt proteins are associated with tumorigenesis, and are present in numerous human breast cancers. Mature human Wnt-1 is a glycosylated protein containing 343 amino acid residues. Recombinant Human Wnt-1 is a 38.4 kDa, non-glycosylated protein containing 343 amino acid residues.

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IL-1α is a non-secreted, proinflammatory cytokine produced in a variety of cells, including monocytes, tissue macrophages, keratinocytes, and other epithelial cells. Both IL-1α and IL-1β bind to the same receptor and have similar, if not identical, biological properties. These cytokines have a broad range of activities including the stimulation of thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, mitogenic FGF-like activity and the release of prostaglandin and collagenase from synovial cells. However, whereas IL-1β is a secreted cytokine, IL-1α is predominantly a cell-associated cytokine. Recombinant Human IL-1α is an 18.0 kDa protein containing 159 amino acid residues.

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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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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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G-CSF is a hematopoietic growth factor that stimulates the development of committed progenitor cells to neutrophils and enhances the functional activities of the mature end-cell. It is produced in response to specific stimulation by a variety of cells, including macrophages, fibroblasts, endothelial cells and bone marrow stroma. G-CSF is being used clinically to facilitate hematopoietic recovery after bone marrow transplantation. Recombinant Rat G-CSF is a 21.6 kDa protein consisting of 196 amino acid residues.