TGF-beta2 (mouse, recombinant)

TGF-beta2 is a multifunctional cytokine and member of the TGF-beta superfamily. It is a ubiquitously expressed proprotein that is cleaved in the endoplasmic reticulum to form TGF-beta2 latency-associated peptide (LAP) and mature TGF-beta2. LAP and TGF-beta2 remain non-covalently bound until mature TGF-beta2 is released into the extracellular matrix from a latency complex by various proteins, including matrix metalloproteinases (MMPs), plasmin, and prostate-specific antigen (PSA). TGF-beta2 binds to TGF-beta receptor type 3 (TGFBR3), which recruits TGFBR2 and ALK5, also known as TGF-betaRI, to induce canonical signaling through SMAD2/3 or non-canonical signaling through various pathways, including PI3K/Akt/mTOR, ERK1/2, or JNK. It is involved in diverse biological processes, including cell differentiation, embryonic development of the heart and motor system, immune system regulation, and glucose tolerance, as well as tumorigenesis. Mutations in TGFB2 are associated with thoracic aortic aneurysms. Cayman's TGF-beta2 (mouse, recombinant) protein consists of 406 amino acids, has a calculated molecular weight of 46. kDa, and a predicted N-terminus of Ser20 after signal peptide cleavage.. Protein function: Transforming growth factor beta-2 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute the regulatory and active subunit of TGF-beta-2, respectively. [The UniProt Consortium]