TGF-beta3 Receptor-Binding Domain (human, recombinant)

TGF-beta3 is a multifunctional cytokine and member of the TGF-beta superfamily. TGF-beta3 is expressed as a proprotein that is cleaved in the Golgi to form TGF-beta3 latency-associated peptide (LAP) and mature TGF-beta3. TGF-beta3 and TGF-beta3 LAP remain non-covalently bound until mature TGF-beta3 is released from latency by various proteins, including matrix metalloproteinases and plasmin. Secreted TGF-beta3 homodimers induce signaling through activin receptor-like kinase 5 (ALK5), also known as TGF-beta receptor type 1 (TGF-betaRI), and TGF-beta receptor type 2 (TGFBR2) and is involved in embryonic development, epidermal homeostasis, wound healing, bone formation, and involution of excess mammary gland epithelial cells during lactation. It increases collagen levels in primary human foreskin fibroblasts. High levels of TGF-beta3 are associated with disease progression in patients with osteosarcoma. Cayman's TGF-beta3 Receptor-Binding Domain (human, recombinant) protein is a disulfide-linked homodimer. The reduced monomer, composed of TGF-beta3 (amino acids 301-412) fused to human IgG1 Fc at its N-terminus, consists of 373 amino acids and has a calculated molecular weight of 41. kDa.. Protein function: Transforming growth factor beta-3 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-3 (TGF-beta-3) chains, which constitute the regulatory and active subunit of TGF-beta-3, respectively. [The UniProt Consortium]