Latent TGF-B1 (human, recombinant)

Transforming growth factor B1 (TGF-B1) is a multifunctional cytokine and member of the TGF-B superfamily.{53547,53548} 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-B. TGF-B1 is expressed as a proprotein that is cleaved in the Golgi to form a latency-associated peptide (LAP) and mature TGF-B1.{53548} LAP and TGF-B1 remain non-covalently bound until mature TGF-B1 is released from latency by various proteins, including matrix metalloproteinases and plasmin, to regulate immune function, epithelial-mesenchymal transition, and cell proliferation. Severe acute respiratory syndrome coronavirus (SARS-CoV) papain-like protease induces TGF-B1-dependent type I collagen production, a marker of pulmonary fibrosis, in A549 cells and mouse lung.{53549} Expression of constitutively active TGF-B1 induces Alzheimer’s disease-like cerebrovascular stiffness and vascular hypertrophy in mice.{53550} Serum and urine levels of TGF-B1 are increased in patients with type 2 diabetes.{53551} Cayman's TGF-B1 (human, recombinant) protein can be used for ELISA, Western blot, and cell-based assay applications. The LAP-bound form of this protein consists of 370 amino acids and has a calculated molecular weight of 42.4 kDa. By SDS-PAGE, under reducing conditions, the apparent moleular mass of the protein is 16, 38, and 55 kDa for mature TGF-B1, LAP, and LAP-bound TGF-B1, respectively, due to glycosylation.