"Peprotech"

Supplier: Peprotech

Monoclonal AntibodyProduced in BALB/c x ICR F1-mice immunized with highly pure Recombinant Human IL-12. Anti­Human IL-12­specific antibody was purified from ascites fluid by Protein A affinity chromatography.

Supplier: Peprotech

Produced from sera of goats immunized with highly pure Recombinant Human SCGF-β. Anti­Human SCGF-β­specific antibody was purified by affinity chromatography employing an immobilized Human SCGF-β matrix.

Supplier: Peprotech

Monoclonal AntibodyProduced in Sprague Dawley rats immunized with highly pure Recombinant Murine IL-12. Anti­Murine IL-12­specific antibody was purified from ascites fluid by Protein A affinity chromatography.

Supplier: Peprotech

Thymosin-β4 is a small, actin-sequestering protein belonging to the thymosin-β family that is found at high concentrations within the spleen, thymus, and peritoneal macrophages, where it is most notably responsible for the organization of cytoskeletal structure. In mammalian tissues, this protein acts as a modulator for the polymerization/depolymerization of actin through the formation of a 1:1 complex with the monomer G (globular)-actin, and inhibits actin’s polymerization to form F (filamentous) actin, which together with other proteins binds microfilaments to construct the cytoskeleton. Commonly found at significant quantities within the brain, lungs, liver, kidneys, testes, and heart, Thymosin-β4 has also been shown to be synthesized by cells unrelated to the reticuloendothelial system, such as myoblasts and fibroblasts, and expressed at irregular levels by several hemopoietic cell lines, malignant lymphoid cells and myeloma cells. In addition to regulating actin polymerization, research has also found Thymosin-β4 to stimulate the secretion of hypothalamic luteinizing hormone-releasing hormone and luteinizing hormone, inhibit the migration of peritoneal macrophages, induce phenotypic changes in T cell lines during early host defense mechanisms, and inhibit the progression of hematopoietic pluripotent stem cells into the s-phase. Recombinant Human/Murine/Rat Thymosin-β4 is a 5.2 kDa glycoprotein containing 45 amino acid residues.

Supplier: Peprotech

Produced from sera of goats immunized with highly pure Recombinant Rat IL-3β. Anti­Rat IL-3β­specific antibody was purified by affinity chromatography and then biotinylated.

Supplier: Peprotech

The FGF family plays a central role during prenatal development, postnatal growth, and the regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-23, FGF-21 and FGF-19 constitute an atypical FGF subfamily whose ligands act as circulating hormones and require the participation of a Klotho protein as a co-receptor for their signaling. FGF-23 is a bone-derived hormone that acts in the kidney to regulate phosphate homeostasis and vitamin D metabolism. The signaling receptor for FGF-23, a Klotho-FGFR1 (IIIc) complex, is an essential regulator of the renal sodium phosphate co-transporter and key vitamin D-metabolizing enzymes CYP27B1 and CYP24A1. Recombinant Murine FGF-23 is a 25.5 kDa globular protein containing 228 amino acid residues.

Supplier: Peprotech

The MCP proteins are members of the CC chemokine family that signal through CCR2 and, with the exception of MCP-1, other CCR receptors. The MCP proteins chemoattract and activate monocytes, activated T cells, basophils, NK cells, and immature dendritic cells. The MCP family cross-reacts across species. Recombinant Murine JE/MCP-1 (CCL2) is a 13.8 kDa protein containing 125 amino acid residues, including the four highly conserved cysteine residues present in the CC chemokines.

Supplier: Peprotech

IFN-γ is an acid-labile interferon produced by CD4 and CD8 T lymphocytes, as well as activated NK cells. IFN-γ receptors are present in most immune cells, which respond to IFN-γ signaling by increasing the surface expression of class I MHC proteins. This promotes the presentation of antigen to T-helper (CD4+) cells. IFN-γ signaling in antigen-presenting, cells and antigen-recognizing B and T lymphocytes, regulates the antigen-specific phases of the immune response. Additionally, IFN-γ stimulates a number of lymphoid cell functions, including the anti-microbial and anti-tumor responses of macrophages, NK cells, and neutrophils. Human IFN-γ is species-specific and is biologically active only in human and primate cells. Recombinant Murine IFN-γ is a 15.6 kDa protein containing 134 amino acid residues.

Supplier: Peprotech

The R-Spondin (Rspo) proteins belong to the Rspo family of Wnt modulators. Currently, the family consists of four structurally-related, secreted ligands (Rspo 1-4), all containing furin-like and thrombospondin structural domains. The Rspo proteins can interact with the Frizzled/LRP6 receptor complex in a manner that causes the stabilization, and resulting accumulation, of the intracellular signaling protein, β-catenin. This activity effectively activates and increases the subsequent nuclear signaling of β-catenin. R-Spondin can also bind to the previously discovered G-protein coupled receptors, LGR-4 and LGR-5. Rspo/β-catenin signaling can act as an inducer of the transformed phenotype, and can also regulate the proliferation and differentiation of certain stem cell populations. Recombinant Human R-Spondin-3 is a 26.9 kDa protein consisting of 240 amino acid residues. Due to glycosylation, R-Spondin-3 migrates at an apparent molecular weight of approximately 37.0 kDa by SDS PAGE analysis under reducing conditions.

Supplier: Peprotech

Produced from sera of rabbits immunized with highly pure Recombinant Human MIP-3β (CCL19). Anti­Human MIP-3β (CCL19)­specific antibody was purified by affinity chromatography employing an immobilized Human MIP-3β matrix.

Supplier: Peprotech

Chemerin is a secreted chemoattractant protein that can signal through the chemokine-like receptor-1 (CMKLR1). It is expressed in various tissues, including white adipose tissue, and circulates in blood as an inactive 143 amino acid precursor protein. Biologically active Chemerin is generated by proteolytic removal of C-terminal residues by several circulating proteases. Chemerin acts as a chemoattractant for cells expressing the CMKLR1 receptor, which includes certain dendritic cells, macrophages, and adipocytes. Recombinant Human Chemerin is a 15.6 kDa protein consisting of 135 amino acid residues.

Supplier: Peprotech

NAP-2 is a CXC chemokine that can signal through the CXCR1 and CXCR2 receptors. It is produced in leukocytes by enzymatic processing of a precursor called platelet basic protein (PBP). NAP-2 chemoattracts and activates neutrophils. Recombinant Human NAP-2 protein is a 7.6 kDa protein containing 70 amino acid residues, including the four highly conserved cysteine residues present in CXC chemokines, and also the "ELR" motif, common to CXC chemokines that bind to CXCR1 and CXCR2.

Supplier: Peprotech

ICAMs are members of the Ig superfamily of calcium-independent transmembrane glycoproteins. ICAM-1 is a ligand for the lymphocyte function-associated antigen (LFA) and Mac-1 integrins, as well as the major human rhinovirus receptor. The primary function of ICAM-1 is to provide adhesion between endothelial cells and leukocytes after stress or injury. The human ICAM-1 gene codes for a 505 amino acid transmembrane glycoprotein containing a 29 amino acid cytoplasmic domain, a 23 amino acid transmembrane domain, and a 453 amino acid extracellular domain. Recombinant Human ICAM-1 is a 49.5 kDa glycoprotein comprising the extracellular domain (453 amino acid residues) of ICAM-1. Monomeric glycosylated ICAM-1 migrates at an apparent molecular weight of approximately 72.0-80.0 kDa by SDS-PAGE analysis under reducing conditions.

Supplier: Peprotech

Proteins of this family play an important role in inducing non-specific resistance against a broad range of viral infections. They also affect cell proliferation and modulate immune responses. Produced by peripheral blood leukocytes and lymphoblastoid cells, IFN-α is an acid-stable molecule that signals through IFN-α/βR, which is also used by IFN-β. Both IFNs have similar anti-viral activity and regulate expression of MHC class I antigens. IFN-α contains four highly conserved cysteine residues that form two disulfide bonds, one of which is necessary for biological activity. PeproTech’s Recombinant Human IFN-β is a 20.0 kDa protein containing 166 amino acid residues. Due to glycosylation, IFN-β has an approximate MW of 22.3 kDa based on SDS-PAGE gel and Mass Spectrometry.

Supplier: Peprotech

The IL-2 receptor system consists of three non-covalently linked subunits termed IL-2Ralpha, IL-2Rbeta, and IL-2Rgamma. The IL-2Ralpha is a type I transmembrane protein consisting of a 219 amino acid extracellular domain, a 19 amino acid transmembrane domain and a 13 amino acid intracellular domain, which is not involved in the transduction of IL-2 signals. Proteolytic processing of IL-2Ralpha releases the entire extracellular domain of IL-2Ralpha, thereby generating a 219 amino acid soluble protein called soluble IL-2Ralpha (sIL-2Ralpha). The homodimeric form binds IL-2 (KD=10mM) and facilitates IL-2 signaling. The secreted sIL-2Ralpha is expressed on leukemia cells, lymphoma cells, and newly activated T and B cells, as well as on approximately 10% of NK cells. Recombinant Human sIL-2 Receptor alpha is a 24.8 kDa protein containing 219 amino acid residues consisting of only the extracellular domain of IL-2Ralpha. As a result of glycosylation, Recombinant Human sIL-2 Receptor alpha migrates with an apparent molecular mass of approximately 40-50 kDa by SDS-PAGE gel, under reducing and non-reducing conditions.

Supplier: Peprotech

IFN-γ is an acid-labile interferon produced by CD4 and CD8 T lymphocytes, as well as activated NK cells. IFN-γ receptors are present in most immune cells, which respond to IFN-γ signaling by increasing the surface expression of class I MHC proteins. This promotes the presentation of antigen to T-helper (CD4+) cells. IFN-γ signaling in antigen-presenting, cells and antigen-recognizing B and T lymphocytes, regulates the antigen-specific phases of the immune response. Additionally, IFN-γ stimulates a number of lymphoid cell functions, including the anti-microbial and anti-tumor responses of macrophages, NK cells, and neutrophils. Human IFN-γ is species-specific and is biologically active only in human and primate cells. Recombinant Murine IFN-γ is a 15.6 kDa protein containing 134 amino acid residues.