Greater than 95.0% as determined by SDS-PAGE.
TGF-β 3 Mouse Recombinant produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide chain containing two 113 amino acid chains and having a total molecular mass of 25.7kDa.
The TGF-β 3 is purified by standard chromatographic techniques.
Recombinant Mouse TGF-β3, produced in E. coli, is a non-glycosylated, homodimeric polypeptide chain connected by disulfide bonds. It comprises two chains of 113 amino acids, resulting in a total molecular weight of 25.7 kDa.
Purification of TGF-β3 is achieved through standard chromatographic methods.
The solution containing the Mouse TGFB3 protein is prepared with 20% Ethanol and 10mM Acetic acid.
SDS-PAGE analysis indicates a purity greater than 95.0%.
MALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.
Recombinant mouse TGF-β3 is a non-glycosylated, disulfide-linked homodimer, consisting of two 112 amino acid chains, with a total molecular weight of approximately 25.5 kDa . The protein is expressed in various tissues and plays a crucial role in cellular adhesion and extracellular matrix (ECM) formation .
TGF-β3 binds to serine-threonine kinase type I and II receptors on the cell surface, initiating a signal transduction cascade through SMAD2/3 proteins . This signaling pathway regulates a variety of cellular functions, including:
TGF-β3 is involved in several critical biological processes:
Recombinant TGF-β3 has been studied for its potential therapeutic applications. For instance, it has been investigated for its role in promoting scar-free healing and improving glucose tolerance . However, clinical trials have shown mixed results, with some promising outcomes in early-phase trials but failures in later phases .