Tgm2, also known as protein-glutamine gamma-glutamyltransferase 2 is calcium dependent enzyme of the protein-glutamine gamma-glutamyltransferases family. Like other transglutaminases, it crosslinks proteins between an epsilon-amino group of a lysine residue and a gamma-carboxamide group of glutamine residue, creating an inter- or intramolecular bond that is highly resistant to proteolysis (protein degradation). Aside from its crosslinking function, tTG catalyzes other types of reactions including deamidation, GTP-binding/hydrolyzing, and isopeptidase activities. unlike other members of the transglutaminase family, tTG can be found both in the intracellular and the extracellular spaces of various types of tissues and is found in many different organs including the heart, the liver, and the small intestine. Recombinant mouse Tgm2 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.