Transforming growth factor β1 (TGF-β1) is a multifunctional cytokine and member of the TGF-β superfamily.1,2 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-β. TGF-β1 is expressed as a proprotein that is cleaved in the Golgi to form TGF-β1 latency-associated peptide (LAP) and mature TGF-β1.2 TGF-β1 LAP and TGF-β1 remain non-covalently bound until mature TGF-β1 is released from latency by various proteins, including matrix metalloproteinases and plasmin, to regulate immune function, epithelial-mesenchymal transition, and cell proliferation. TGF-β1 LAP inhibits TGF-β1-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.3,4 Cayman’s TGF-β1 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.WARNING This product is not for human or veterinary use.
