TGF-beta1 LAP (human, recombinant)

Transforming growth factor beta1 (TGF-beta1) is a multifunctional cytokine and member of the TGF-beta superfamily. It is an extracellular dimeric protein that is produced by multiple cell types, including macrophages, platelets, neutrophils, regulatory T cells, and renal tubular cells, and is the most abundantly expressed isoform of TGF-beta. TGF-beta1 is expressed as a proprotein that is cleaved in the Golgi to form TGF-beta1 latency-associated peptide (LAP) and mature TGF-beta1. TGF-beta1 LAP and TGF-beta1 remain non-covalently bound until mature TGF-beta1 is released from latency by various proteins, including matrix metalloproteinases and plasmin, to regulate immune function, epithelial-mesenchymal transition, and cell proliferation. TGF-beta1 LAP inhibits TGF-beta1-induced inflammation and fibrosis in HSC-T6 rat hepatic cells and H9c2 rat cardiomyocytes, as well as in a mouse model of carbon tetrachloride-induced liver fibrosis. Cayman's TGF-beta1 LAP (human, recombinant) protein consists of 260 amino acids, has a calculated molecular weight of 29.9 kDa, and a predicted N-terminus of Leu30 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is ~38-45 kDa due to glycosylation.Synonyms: TGF-beta1 Latency-associated Peptide, Transforming Growth Factor beta1 LAP, Transforming Growth Factor beta1 Latency-associated Peptide. Purity: >95% as estimated by SDS-PAGE. Endotoxin Testing: <1.0 EU/µg determined by the LAL endotoxin assay. Source: Recombinant human C-terminal His-tagged TGF-beta1 LAP expressed in HEK293 cells. Amino Acids: 1-278 (full length). MW: 29.9 kDa. Formulation: (Request formulation change), Lyophilized from sterile PBS, pH 7.4.