TGFB3 (24-412 a.a.) corresponds to the proprotein region after cleavage of the 20 a.a. signal peptide. It includes:
Latency-associated peptide (LAP): 24-220 a.a., regulates TGFB3 activation .
Mature TGFB3: 301-412 a.a., the bioactive domain responsible for receptor binding .
TGFB3 regulates:
Embryogenesis: Critical for palatogenesis, pulmonary development, and cardiac morphogenesis .
Wound healing: Accelerates repair by modulating cell adhesion and extracellular matrix synthesis .
Immune regulation: Inhibits IL-4-dependent T-cell proliferation (ED50: 40 ng/ml) .
TGFB3 (24-412 a.a.) is produced in multiple systems with varying characteristics:
Genetic mutations: Heterozygous TGFB3 mutations (e.g., c.754+2T>C) cause syndromic aortic aneurysms, mitral valve disease, and skeletal abnormalities .
Therapeutic potential:
Signaling paradox: Mutations upregulate canonical (Smad2/3) and noncanonical (ERK, JNK) TGF-β pathways, contributing to vascular pathology .
The human recombinant TGF-β3 (24-412 a.a.) is produced in E. coli and consists of a single, non-glycosylated polypeptide chain containing 412 amino acids, with a molecular mass of approximately 47.2 kDa . This recombinant protein is fused to a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques .
TGF-β3 plays a crucial role in various biological processes, including:
Mutations in the TGFB3 gene are associated with several medical conditions, including:
Recombinant TGF-β3 is widely used in research to study its role in various cellular processes and its potential therapeutic applications. Despite its promising effects in preclinical studies, human recombinant TGF-β3 (avotermin) failed in Phase III clinical trials for wound healing .
In summary, TGF-β3 is a vital cytokine with significant roles in cell differentiation, embryogenesis, and wound healing. Its recombinant form, produced in E. coli, is a valuable tool for scientific research and potential therapeutic applications.