Anti-Transglutaminase-2 Antibody, FN binding domain Antibody, clone 4G3 clone 4G3, from mouse

Protein-glutamine gamma-glutamyltransferase 2 (UniProt: P21980; also known as EC: 2.3.2.13, Tissue transglutaminase, Transglutaminase C, TG(C), TGC, TGase C, Transglutaminase H, TGase H, Transglutaminase-2, TGase-2, TG2) is encoded by D13the TGM2 gene (Gene ID: 7052) in human. TG2 is a multi-domain, multi-functional enzyme that is shown to post-translationally modify proteins by catalyzing the formation of intermolecular isopeptide bonds between glutamine and lysine side-chains. It catalyes the calcium-dependent covalent modification of protein-bound glutamine side chains through transamidation or deamidation reactions. Recycling endosomes is reported to be essential for externalization of TG2, which does not follow the classical ER/Golgi-dependent secretion pathway, but is targeted to perinuclear recycling endosomes, and is delivered inside these vesicles prior to externalization. Inactivation of recycling endosomes or blocking endosome fusion with the plasma membrane is shown to block TG2 secretion. TG2 plays a critical role in extracellular matrix formation and integrin mediated signaling. It is also reported to be involved in cell signaling involving 7-transmembrane receptors. It also participates in the pathogenesis of neurodegenerative diseases and certain cancers. (Ref.: Zemskov, EA., et al (2011). PLoS ONE 6(4): e19414; Siegal, M., and Khosla, C. (2007). Pharmacol. Ther. 115(2); 232-245.