Tissue transglutaminase, also known as transglutaminase 2 (TG2), is a multifunctional enzyme that belongs to the family of protein-glutamine γ-glutamyltransferases . This enzyme is involved in various physiological processes, including protein cross-linking, cell signaling, and apoptosis . The recombinant form of tissue transglutaminase from mice is widely used in research to study its functions and regulatory mechanisms.
Tissue transglutaminase is a 78-kDa, calcium-dependent enzyme that catalyzes the formation of covalent bonds between an ε-amino group of a lysine residue and a γ-carboxamide group of a glutamine residue . This cross-linking activity is crucial for stabilizing protein structures and is highly resistant to proteolysis . Additionally, tissue transglutaminase exhibits guanosine 5′-triphosphate (GTP) hydrolysis activity, protein disulfide isomerase activity, and protein kinase activity .
Tissue transglutaminase is involved in several physiological processes, including:
The recombinant form of tissue transglutaminase from mice is produced using genetic engineering techniques. The gene encoding tissue transglutaminase is cloned into an expression vector, which is then introduced into a suitable host cell, such as Escherichia coli or mammalian cells . The host cells are cultured under optimal conditions to express the recombinant protein, which is subsequently purified using chromatographic techniques .
Recombinant tissue transglutaminase is used in various research applications, including: