Tissue Transglutaminase

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Tissue Transglutaminase

Product description:Tissue transglutaminase (abbreviated as TG2 or tTG) is an enzyme of the transglutaminase family. Like other transglutaminases, it crosslinks proteins between an ε-amino group of a lysine residue and a γ-carboxamide group of glutamine residue, creating an inter- or intramolecular bond that is highly resistant to proteolysis (protein degradation). It is particularly notable for being the autoantigen in coeliac disease, but is also known to play a role in apoptosis, cellular differentiation, and matrix stabilisation.
Application:tTG is expressed ubiquitously. It requires calcium as a cofactor for transamidation activity. Transcription is increased by retinoic acid. Among its many supposed functions, it appears to play a role in wound healing, apoptosis, and extracellular matrix development.
TG2 also has GTPase activity: In the presence of GTP, it suggested to function as a G protein participating in signaling processes.Besides its transglutaminase activity, TG2 is proposed to also act as kinase,and protein disulfide isomerase,[4] and deamidase.This latter activity is important in the deamidation of gliadin peptides, thus playing important role in the pathology of coeliac disease.
Recent studies suggest that tTG plays a role in inflammation, degenerative diseases, and tumor biology.

 

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