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Catalog Number: (10771-558)

Supplier: Peprotech

Description: PeproTech's Human GRO-β (CXCL2) ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant human GRO-β (CXCL2) in a sandwich ELISA format.

Catalog Number: (10771-660)

Supplier: Peprotech

Description: PeproTech's Human IL-8 (CXCL8) ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant human IL-8 (CXCL8) in a sandwich ELISA format.

Catalog Number: (10771-656)

Supplier: Peprotech

Description: PeproTech's Human IL-4 ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant human IL-4 in a sandwich ELISA format.

Catalog Number: (10771-614)

Supplier: Peprotech

Description: PeproTech's Human CTACK (CCL27) ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant human CTACK (CCL27) in a sandwich ELISA format.

Supplier: Peprotech

Description: 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 Human SDF-1α (CXCL12) is an 8.0 kDa protein containing 68 amino acid residues.

Catalog Number: (10771-688)

Supplier: Peprotech

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-I is 7.6 kDa.

Supplier: Peprotech

Description: FGF-18 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-18 is an essential regulator of long bone and calvarial development. FGF-18 signals through FGFR 1c, 2c, 3c, and 4. Recombinant Human FGF-18 derived from

Supplier: Peprotech

Description: FGF-10 is a heparin-binding growth factor that belongs to the FGF family.

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Supplier: Peprotech

Description: SCGF-α and -β are hematopoietic growth factors that exert their activity at early stages of hematopoiesis. The SCGFs are non-glycosylated, species-specific cytokines that can support growth of primitive hematopoietic cells, and, in combination with EPO or GM-CSF, promote proliferation of erythroid or myeloid progenitors, respectively. Recombinant Human SCGF-α is a 33.9 kDa polypeptide containing 305 amino acid residues.

Supplier: Peprotech

Description: Betacellulin is an EGF-related polypeptide growth factor that signals through the EGF receptor. It is produced in several tissues, including the pancreas, small intestine, and in certain tumor cells. Betacellulin is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. Human Betacellulin is initially synthesized as a glycosylated 32.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce the mature sequence. Recombinant Human Betacellulin is a 9.0 kDa monomeric protein, containing 80 amino acid residues, which comprises the mature EGF-homologous portion of the Betacellulin protein.

Supplier: Peprotech

Description: Thrombomodulin (TM, CD141, THBD) is an endothelial cell-expressed, transmembrane glycoprotein that can form a complex with the coagulation factor, thrombin. The thrombomodulin/thrombin complex converts protein C to its activated form, protein Ca, which in turn proteolytically cleaves and deactivates factor Va and factor VIIIa, two essential components of the coagulation mechanism. This inactivation reduces the generation of additional thrombin, and thereby effectively prevents continued coagulation. Reduced levels of thrombomodulin can correlate with the pathogenesis of certain cardiovascular diseases, such as atherosclerosis and thrombosis. However, the serum levels of the truncated circulating form of thrombomodulin are typically elevated during inflammation and in the presence of various inflammatory-related diseases. The thrombomodulin protein contains 575 amino acids, including an 18 a.a. signal sequence, a 497 a.a. extracellular domain, a 24 a.a. transmembrane sequence, and a 36 a.a. cytoplasmic region. Recombinant Human Thrombomodulin is a 51.4 kDa, 491-amino-acid length glycoprotein containing the extracellular domain of thrombomodulin.

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Supplier: Peprotech

Description: Myostatin is a TGF-β family member that acts as an inhibitor of skeletal muscle growth. This muscle-specific cytokine interacts with Activin type I and type II receptors, and suppresses myoblast proliferation by arresting cell-cycle in the G1 phase. Suppression of myostatin activity facilitates muscle formation, and may be useful in reducing and/or preventing adiposity and type-2 diabetes. Myostatin activity can be blocked by the activin-binding protein follistatin, and by the propeptide of myostatin. The amino acid sequence of mature myostatin is extremely conserved across species, and is the same in murine, rat, chicken, turkey, porcine, and human. Myostatin is expressed as the C-terminal part of a precursor polypeptide, which also contains a short N-terminal signal sequence for secretion, and a propeptide of 243 amino acids. After dimerization of this precursor, the covalent bonds between the propeptide and the mature ligand are cleaved by furin-type proteases. However, the resulting two proteins remain associated through non-covalent interactions, and are secreted as a latent complex. Recombinant Human/Murine/Rat Myostatin is a 25.0 kDa protein consisting of two identical 109 amino acid polypeptides linked by a single disulfide bond.

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Supplier: Peprotech

Description: Vimentin is a class III intermediate filament protein predominantly found in cells of mesenchymal origins, such as vascular endothelium and blood cells, where it functions as a major cytoskeletal component. Due to its importance and abundance in the cytoskeletal structure of mesenchymally-derived cells, vimentin is frequently used as a developmental marker within cells of mesenchymal origin or cells undergoing epithelial-mesenchymal transition, which can occur during both normal and metastatic growth. An active participant within several critical processes of cellular organization and protein regulation, vimentin is involved in the anchorage of organelles within the cytoplasmic matrix, development of astrocytes, and the disassembly of cellular components during the execution phase of apoptosis. Abnormalities in the normal physiological pathways of vimentin have been implicated in deficient motility and directional migration involved in wound healing, cellular growth and development, as well as the adhesion-site accumulation of vimentin on lens epithelial cells in cases of dominant cataracts. Recombinant Human Vimentin is a 54.3 kDa protein consisting of 471 amino acid residues, including a 6-residue C-terminal His-Tag.

Supplier: Peprotech

Description: SPARC/Osteonectin is a secreted, evolutionarily-conserved, collagen-binding glycoprotein that is involved in a variety of cellular activities. It is highly expressed in tissues undergoing morphogenesis, remodeling and wound repair. SPARC/Osteonectin and its related peptides bind to numerous proteins of the extracellular matrix (ECM), affect ECM protein expression, influence cellular adhesion and migration, and modulate growth factor-induced cell proliferation and angiogenesis. SPARC/Osteonectin consists of three domains: an N-terminal acidic region that binds calcium ions with low affinity, a module containing two EF-hand motifs that bind calcium with high affinity, and a cysteine-rich follistatin-like domain. Recombinant Human SPARC/Osteonectin is a glycoprotein containing 286 amino acids that migrates at an apparent MW of 43.7 kDa by SDS-PAGE analysis due to the effect of glycosylation. The calculated molecular weight of Recombinant Human SPARC/Osteonectin is 32.7 kDa.

Supplier: Peprotech

Description: CYR61 is a member of the CCN family of secreted cysteine-rich regulatory proteins. CYR61 induces angiogenesis by stimulating the proliferation, migration, and adhesion of endothelial cells. Cell migration and adhesion are mediated through binding to specific cell surface integrins and to heparin sulfate proteoglycans. Increased expression of CYR61 is associated with several types of cancer, and correlates with the progression and estrogen independence of human breast cancers. Recombinant Human CYR61 is a 39.4 kDa protein containing 357 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

Description: Wnt-7a belongs to the Wnt family of signaling proteins that play a key role in maintaining the integrity of embryonic and adult tissues. It is expressed in placenta, kidney, testis, uterus, fetal lung, and fetal and adult brain. Most Wnt proteins can signal though a mechanism called the canonical Wnt pathway, in which Wnt proteins bind to and activate seven-pass transmembrane receptors of the Frizzled family, ultimately leading to the disruption of β-catenin degradation. Intracellular accumulation of β-catenin increases translocation of the protein into the nucleus, where it binds to TCF/LEF transcription factors to induce the expression of numerous genes. Increased Wnt/β-catenin signaling is associated with tumorigenesis in a diverse set of human cancers. However, Wnt-7a/Frizzled-9 signaling has been shown to act as a tumor suppressor in non-small cell lung cancers. Recombinant Human Wnt-7a is a 35.5 kDa glycoprotein containing 318 amino acids. Due to glycosylation, Wnt-7a migrates between 40-55 kDa by SDS-PAGE gel under unreduced conditions.