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Supplier: PeproTech, Inc.

Description: The three mammalian isoforms of TGF-β, TGF-β1, β2, and β3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility, as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes, including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes, which are stored at the cell surface and in the extracellular matrix. The release of the biologically active TGF-β isoform from a latent complex involves proteolytic processing of the complex and /or induction of conformational changes by proteins such as thrombospondin-1. TGF-β1 is the most abundant isoform secreted by almost every cell type. It was originally identified for its ability to induce phenotypic transformation of fibroblasts, and recently it has been implicated in the formation of skin tumors. Recombinant Human TGF-β1 is a 25.0 kDa protein composed of two identical 112 amino acid polypeptide chains linked by a single disulfide bond.

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Supplier: PeproTech, Inc.

Description: The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro . IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant Human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds. The calculated molecular weight of Recombinant Human IGF-II is 7.5 kDa.

Supplier: PeproTech, Inc.

Description: Produced from sera of rabbits immunized with highly pure Recombinant Murine MCP-2 (CCL8). Anti­Murine MCP-2 (CCL8)­specific antibody was purified by affinity chromatography employing an immobilized Murine MCP-2 matrix.

Supplier: PeproTech, Inc.

Description: Produced from sera of rabbits immunized with highly pure Recombinant Murine Exodus-2 (CCL21). Anti­Murine Exodus-2 (CCL21)­specific antibody was purified by affinity chromatography and then biotinylated.

Supplier: PeproTech, Inc.

Description: Produced from sera of rabbits immunized with highly pure Recombinant Murine RELMα. Anti­Murine RELMα­specific antibody was purified by affinity chromatography employing an immobilized Murine RELMα matrix.

Supplier: PeproTech, Inc.

Description: IL-20 is a member of the IL-10 family of regulatory cytokines, which includes IL-10, IL-19, IL-20, IL-22, IL-24 and IL-26. Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. IL-20 is a hematopoietic growth factor capable of stimulating colony formation by CD34+ multipotential progenitors, but not by other progenitor cells. IL-20 signals through a receptor system composed of type I IL-20Rα and type II IL-20Rβ. Over-expression of IL-20 in keratinocytes expressing both receptor subunits has been implicated in the induction of inflammatory skin disease. Recombinant Human IL-20 is a 35.2 kDa homodimeric protein consisting of two 153 amino acid polypeptide chains.

Supplier: PeproTech, Inc.

Description: Produced from sera of rabbits immunized with highly pure Recombinant Human BD-4. Anti­Human BD-4­specific antibody was purified by affinity chromatography and then biotinylated.

Supplier: PeproTech, Inc.

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. 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.  The PBEF gene encodes a polypeptide of 491 amino acid residues. The secreted form of this polypeptide, i.e. visfatin, contains 465 residues and lacks the first 26 N-terminal residues of the PBEF gene product. The 491-residue form has been shown to be a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAD biosynthesis. The amino acid sequence of visfatin is highly conserved across different species and shows no homology to any known protein. It contains 5 cysteine residues, of which only two of them appear to be involved in disulfide bridge formation. Recombinant human Visfatin is a 52.6 kDa protein containing 466 amino acid residues (isoform 1).

Supplier: PeproTech, Inc.

Description: Produced from sera of rabbits immunized with highly pure Recombinant Human sRANK Receptor. Anti­Human sRANK Receptor­specific antibody was purified by affinity chromatography and then biotinylated.

Supplier: PeproTech, Inc.

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).

Supplier: PeproTech, Inc.

Description: FGF-10 is a heparin-binding growth factor that belongs to 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-10 is most related to KGF/FGF-7, and is expressed during the development and, preferentially, in adult lungs. It signals through the FGFR 2b. Recombinant Human FGF-10 is a 19.3 kDa protein consisting of 170 amino acid residues.

Supplier: PeproTech, Inc.

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 an activin antagonist 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.

Supplier: PeproTech, Inc.

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 Human MEC (CCL28) is a 12.3 kDa protein containing 108 amino acid residues.

Supplier: PeproTech, Inc.

Description: 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.

Supplier: PeproTech, Inc.

Description: Produced from sera of rabbits immunized with highly pure Recombinant Murine Eotaxin (CCL11). Anti­Murine Eotaxin (CCL11)­specific antibody was purified by affinity chromatography employing an immobilized Murine Eotaxin matrix.

Supplier: PeproTech, Inc.

Description: FGF-basic 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-basic is a non-glycosylated, heparin-binding growth factor that is expressed in the brain, pituitary, kidney, retina, bone, testis, adrenal gland, liver, monocytes, epithelial cells and endothelial cells. FGF-basic signals through FGFR 1b, 1c, 2c, 3c and 4. Recombinant Human FGF-basic is a 16.4 kDa protein consisting of 146 amino acid residues.