Transglutaminase 3/TGM3 Protein, Human (sf9, His)

Transglutaminase 3 (TGM3) is a multifunctional protein that facilitates the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins. Furthermore, TGM3 is instrumental in the conjugation of polyamines to proteins. The protein is prominently engaged in the creation of the cornified envelope (CE), a specialized structure characterized by covalent cross-links of proteins beneath the plasma membrane in terminally differentiated keratinocytes. TGM3 catalyzes the cross-linking of small proline-rich proteins (SPRR1 and SPRR2) and LOR, leading to the formation of small interchain oligomers. These oligomers are subsequently cross-linked by TGM1 onto the growing CE scaffold, emphasizing TGM3's role in the intricate process of CE assembly. Additionally, TGM3 participates in hair follicles by cross-linking structural proteins, contributing to the reinforcement and hardening of the inner root sheath. This comprehensive functionality underscores TGM3 as a key player in protein cross-linking and structural organization within cellular contexts.