TGFB3 (24-412 a.a.) Human

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:

• Cell Differentiation: It regulates the differentiation of various cell types, contributing to tissue development and repair .
• Embryogenesis: TGF-β3 is essential for proper embryonic development, particularly in the formation of the palate and lungs .
• Wound Healing: It orchestrates the movements of epidermal and dermal cells during the wound healing process .
• Extracellular Matrix Formation: TGF-β3 regulates molecules involved in cellular adhesion and extracellular matrix (ECM) formation .

Mutations in the TGFB3 gene are associated with several medical conditions, including:

• Loeys-Dietz Syndrome 5: A connective tissue disorder characterized by aortic aneurysms and dissections .
• Arrhythmogenic Right Ventricular Dysplasia (ARVD1): A condition affecting the heart’s muscle tissue, leading to arrhythmias .

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.