1636 Results for: "Peprotech"

Supplier: Peprotech

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 Human Resistin is a 19.5 kDa, disulfide-linked, homodimeric protein composed of two identical 92 amino acid chains linked by a single disulfide bond.

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. Enterokinase sequentially cleaves carboxyl side of D-D-D-D-K. Human Enterokinase is expressed as a linear 1019 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of Enterokinase, which consists of two polypeptide chains (heavy chain and light chain) held together by a single disulfide bond, resulting in formation of a biologically active heterodimer. The heavy chain consists of 784 amino acid residues, and the light chain consists of 235 amino acid residues. The calculated molecular weight of Recombinant Human Enterokinase is 108.7 kDa.

Supplier: Peprotech

Produced from sera of rabbits immunized with highly pure Recombinant Human Galectin-1. Anti­Human Galectin-1­specific antibody was purified by affinity chromatography employing an immobilized Human Galectin-1 matrix.

Supplier: Peprotech

Produced from sera of rabbits immunized with highly pure Recombinant Murine IL-22. Anti­Murine IL-22­specific antibody was purified by affinity chromatography and then biotinylated.

Supplier: Peprotech

Produced from sera of rabbits immunized with highly pure Recombinant Human Artemin. Anti­Human Artemin­specific antibody was purified by affinity chromatography and then biotinylated.

Supplier: Peprotech

KGF (FGF-7) is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth, and the regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. KGF (FGF-7) is a mitogen factor specific for epithelial cells and keratinocytes. KGF/FGF-7 signals through FGFR 2b. KGF (FGF-7) plays a role in kidney and lung development, as well as in angiogenesis and wound healing. Recombinant Human KGF (FGF-7) is an 18.9 kDa protein consisting of 163 amino acid residues.

Supplier: Peprotech

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 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 derived from

Supplier: Peprotech

Flt3-Ligand is a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand binds to cells expressing the tyrosine kinase receptor Flt3. Flt3-Ligand, by itself does not stimulate proliferation of early hematopoietic cells, but synergizes with other CSFs and interleukins to induce growth and differentiation. Unlike SCF, Flt3-Ligand exerts no activity on mast cells. Multiple isoforms of Flt3-Ligand have been identified. The predominant biologically active form is anchored to the cell surface as the extracellular domain of a transmembrane protein (209 a.a.). The membrane-bound isoform can be proteolytically cleaved to generate a biologically active soluble isoform. Recombinant Murine Flt3-Ligand is a soluble 18.6 kDa protein consisting of 163 amino acid residues.

Supplier: Peprotech

Noggin belongs to a group of diffusible proteins that bind to ligands of the TGF-β family, and regulate their activity by inhibiting their access to signaling receptors. Noggin was originally identified as a BMP-4 antagonist whose action was critical for proper formation of the head and other dorsal structures. Consequently, noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of noggin in mice results in prenatal death, and a recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant Murine Noggin is a 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.

Supplier: Peprotech

Produced from sera of rabbits immunized with highly pure Recombinant Rat RANTES (CCL5). Anti­Rat RANTES (CCL5)­specific antibody was purified by affinity chromatography and then biotinylated.

Supplier: Peprotech

Murine IL-4, Polyclonal Antibody, source: Rabbit, purified by affinity chromatography, cross reactivity: Mouse, Immunogen: E.coli derived Recombinant Murine IL-4, Application: Elisa, Western Blot, pack size: 50ug

Supplier: Peprotech

Murine IP-10, Polyclonal Antibody, source: Rabbit, purified by affinity chromatography, And then Biotinylated, cross reactivity: Mouse, Immunogen: E.coli derived Recombinant Murine IP-10 (CXCL10), Application: Elisa, Western Blot, pack size: 1mg

Supplier: Peprotech

Recombinant Murine R-Spondin-1, Purity: Greater than 95% by SDS-PAGE gel and HPLC analyses, Source: CHO cells, Cross Reactivity: Mouse, R-Spondin-1 enhances BMP-2-mediated differentiation of MC3T3-E1 cells, Synonyms: Roof plate-specific Spondin-1, Size: 250UG

Supplier: Peprotech

Recombinant Human B7-H2 Fc, Purity: Greater than 95% by SDS-PAGE gel and HPLC analyses, Source: CHO cells, Determined by its ability to induce adhesion in Jurkat cells activated by immobilized anti-CD3, Synonyms: B7-like protein Gl50, CD275, Size: 1MG

Supplier: Peprotech

Produced from sera of rabbits immunized with highly pure Recombinant Human NT-3. Anti­Human NT-3­specific antibody was purified by affinity chromatography and then biotinylated.

Supplier: Peprotech

Animal-Free Human FGF-19 Recombinant Protein, Purity: >95% SDS and HPLC, Source: E.coli, Biological Activity: Determined by a cell proliferation assay using Balb/c 3T3 cells, 100-150 ng/ml, Synonyms: Fib