"Peprotech"

Supplier: Peprotech

PDGFs are disulfide-linked dimers consisting of two 12.0-13.5 kDa polypeptide chains, designated PDGF-A and PDGF-B chains. The three naturally occurring PDGFs, PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types, including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGFs are stored in platelet α-granules, and are released upon platelet activation. The PDGFs are involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGFs have been identified and named PDGFR-α and PDGFR-β. PDGFR-α is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-β interacts with only PDGF-BB and PDGF-AB. Recombinant Human PDGF-AB is a 26.4 kDa disulfide-linked dimer, consisting of one α chain and one β chain (234 total amino acids).

Supplier: Peprotech

The platelet-derived growth factor (PDGF) family of heparin-binding growth factors consists of five known members, denoted PDGF-AA, PDGF-BB, PDGF-AB, PDGF-CC and PDGF-DD. The mature and active form of these proteins, an anti-parallel, disulfide-linked dimer of two 12-14 kDa, polypeptide chains, is obtained through proteolytic processing of biologically inactive precursor proteins, which contain an N-terminal CUB domain and a PDGF/VEGF homologous domain. The PDGFs interact with two related protein tyrosine kinase receptors, PDGFR-α and PDGFR-β, and are potent mitogens for a variety of cell types, including smooth muscle cells, connective tissue cells, bone and cartilage cells, and certain tumor cells. They play an important role in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubules' epithelial cell development. Mature PDGFs are stored in platelet α-granules, and are released upon platelet activation. PDGF-AA, -AB, -BB and -CC signal primarily through the PDGF-Rα receptor, whereas PDGF-DD interacts almost exclusively with the PDGF-Rβ receptor. Recombinant Human PDGF-CC is a 25.0 kDa protein consisting of two identical disulfide-linked, 112 amino acid, polypeptide chains.

Supplier: Peprotech

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 sCD22 is a soluble 75.0 kDa protein which corresponds to the extracellular domain of CD22.

Supplier: Peprotech

Neuregulin/Heregulin is a family of structurally related polypeptide growth factors derived from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4).

Supplier: Peprotech

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, as well as 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.

Supplier: Peprotech

IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. Currently, there are seven named IGF-BPs that form high affinity complexes with both IGF-I and IGF-II. IGF-BP5 is a 28.6 kDa, cysteine-rich, secreted protein produced by vascular smooth muscle cells. It is the major IGF-binding protein present in bone tissue and helps potentiate the action of IGF-I on smooth muscle cells, fibroblasts, and osteoblasts. Data shows that IGFBP-5 acts as a growth inhibitor and pro-apoptotic agent in breast cancer cells. IGFBP-5-overexpressing mice show an increase in neonatal mortality, reduced female fertility, whole-body growth inhibition, and retarded muscle development. Recombinant Human IGF-BP5 is a 28.6 kDa protein consisting of 253 amino acid residues.

Supplier: Peprotech

PlGF-1 is an angiogenic factor that belongs to the cysteine-knot superfamily of growth factors. PlGF-1 is expressed in placental tissues, the colon, and mammary carcinomas. It signals through the VEGFR-1/FLT1 receptor, and stimulates endothelial cell proliferation and migration. Recombinant Human PlGF-1 is a 29.7 kDa disulfide-linked homodimeric protein of two 132 amino acid polypeptide chains.

Supplier: Peprotech

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 immunoegulatory 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 23.0 kDa globular protein containing 200 amino acid residues.

Supplier: Peprotech

IGF-BP3 is a 30 kDa, cysteine-rich secreted protein. It is the major IGF binding protein present in the plasma of human and animals, and it is also found in α-granules of platelets. In addition to its ability to modulate the activity of IGF-I and IGF-II, IGF-BP3 exerts inhibitory effects on follicle stimulating hormone (FSH) activity. Decreased plasma levels of IGF-BP3 often results in dwarfism, whereas elevated levels of IGF-BP3 may lead to acromegaly. The expression of IGF-BP3 in fibroblasts is stimulated by mitogenic growth factors, such as Bombesin, Vasopressin, PDGF, and EGF. Recombinant Human IGF-BP3 is a 28.8 kDa protein consisting of 264 amino acid residues.

Supplier: Peprotech

PTHrP is a polypeptide hormone produced by almost every tissue of the body.

Supplier: Peprotech

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. Recombinant Aeromonas Aminopeptidase is a 31.4 kDa protein containing 291 amino acid residues.

Supplier: Peprotech

Eotaxin-3 is a CC chemokine that signals through the CCR3 receptor. It is produced by endothelial cells stimulated with IL-4 or IL-13. Eotaxin-3 selectively targets cells expressing CCR3, including eosinophils, basophils, T cells and monocytes. Eotaxin-3 has similar activity to Eotaxin and Eotaxin-2, but the three Eotaxins share only a low degree of sequence homology. Recombinant Human Eotaxin-3 (CCL26) is an 8.4 kDa protein containing 71 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.

Supplier: Peprotech

Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors, and are released by proteolytic cleavage of a signal sequence and, in some cases, a propeptide sequence. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant Human BD-2 is a 4.3 kDa protein containing 41 amino acid residues.

Supplier: Peprotech

Breast and Kidney-expressed chemokine (BRAK) is a CXC chemokine expressed in normal tissue in the absence of inflammatory stimuli, and infrequently expressed in cancer cell lines. BRAK is known to be a highly selective monocyte chemoattractant. However, main function and receptor selectivity is unknown at this time. BRAK contains the four highly conserved cysteine residues present in CXC chemokines. The sequence of the mature protein consists of 87 amino acid residues, and is approximately 30% homologous to the sequences of MIP-2 alpha and beta. Recombinant Human BRAK (CXCL14) is a 9.4 kDa protein containing 77 amino acid residues.

Supplier: Peprotech

Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors, and are released by proteolytic cleavage of a signal sequence and, in some cases, a propeptide sequence. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant Human BD-1 is a 3.9 kDa protein containing 36 amino acid residues.

Supplier: Peprotech

Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors, and are released by proteolytic cleavage of a signal sequence and, in some cases, a propeptide sequence. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant Human BD-1 is a 5.0 kDa protein containing 47 amino acid residues.