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Supplier: Peprotech

Description: Resistin belongs to a family of tissue-specific cytokines termed FIZZ (found in inflammatory zones) and RELM. The four known members of this family, resistin, RELMα, RELMβ, and RELMγ, 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. Resistin is an adipose-derived cytokine (adipokine) whose physiological function and molecular targets are largely unknown. Studies have shown that resistin suppresses insulin's ability to stimulate glucose uptake, and postulated that resistin might be an important link between obesity and Type 2 diabetes. Other studies have indicated that resistin expression is severely suppressed in obesity, and that it may act as a feedback regulator of Adipogenesis. Recombinant Rat Resistin is a 20.0 kDa, disulfide-linked, homodimeric protein composed of two 94 identical amino acid chains linked by a single disulfide bond.

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: GLP-1 is a proglucagon-derived peptide hormone secreted primarily by intestinal L cells during feeding. Its major physiological function is the stimulation of pancreatic β cells to release appropriate amounts of insulin after glucose absorption. Other biological actions exhibited by GLP-1 include the suppression of plasma glucagon levels, inhibition of gastric motility, and promotion of satiety. The secretion of GLP-1 from intestinal L cells is stimulated by nutrients, hormones, and neural inputs. On the other hand, insulin has been reported to inhibit GLP-1 release, indicating that a feedback loop mechanism regulates GLP-1 secretion. In addition to being the precursor of GLP-1, proglucagon, whose primary structure is highly conserved in mammalian species, is also the precursor for other members of the glucagon family of peptide hormones, including glicentin-related pancreatic peptide (GRPP), glucagons, and GLP-2. Recombinant Human GLP-1 is a 3.3 kDa polypeptide consisting of 31 amino acid residues.

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.

Supplier: Peprotech

Description: Anti-IgG Rabbit Polyclonal Antibody Artemin

Supplier: Peprotech

Description: Produced from sera of rabbits immunized with highly pure Recombinant Human IL-17B. Anti­Human IL-17B­specific antibody was purified by affinity chromatography employing an immobilized Human IL-17B matrix.

Supplier: Peprotech

Description: Produced from sera of rabbits immunized with highly pure Recombinant Human IL-17B. Anti­Human IL-17B­specific antibody was purified by affinity chromatography and then biotinylated.

Supplier: Peprotech

Description: 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 the 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 Human VEGF

Supplier: Peprotech

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

Description: Produced from sera of goats immunized with highly pure Recombinant Human Resistin. Anti­Human Resistin­specific antibody was purified by affinity chromatography employing an immobilized Human Resistin matrix.

Supplier: Peprotech

Description: Produced from sera of goats immunized with highly pure Recombinant Human Resistin. Anti­Human Resistin­specific antibody was purified by affinity chromatography and then biotinylated.

Supplier: Peprotech

Description: Produced from sera of rabbits immunized with highly pure Recombinant Murine MDC (CCL22). Anti­Murine MDC (CCL22)­specific antibody was purified by affinity chromatography and then biotinylated.

Supplier: Peprotech

Description: 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 Rat PlGF-1 is a 30.3 kDa disulfide-linked homodimeric protein of two 135 amino acid polypeptide chains.

Supplier: Peprotech

Description: Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-2 is a secreted collagenase with specificity toward Type IV, V, VII, and X collagens. Recombinant Human MMP-2 is a 62.0 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (552 amino acids).

Supplier: Peprotech

Description: Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-3 degrades fibronectin, laminin, collagens III, IV, and X, and cartilage proteoglycans. Recombinant Human MMP-3 is a 42.8 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (378 amino acids).

Supplier: Peprotech

Description: 32238807