Transglutaminase-2 (TG2) Antibody – Mouse Monoclonal

Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

TGM2: an enzyme of the transglutaminase family that catalyzes the crosslinking of proteins and the conjugation of polyamines to proteins. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. . Is the autoantigen in coeliac disease and plays a role in apoptosis, cellular differentiation and matrix stabilisation. Three alternatively spliced isoforms have been described.

Protein type: EC 2.3.2.13; Transferase

Chromosomal Location of Human Ortholog: 20q12

Cellular Component: cytosol; endoplasmic reticulum; focal adhesion; intrinsic to plasma membrane; mitochondrion

Molecular Function: metal ion binding; protein binding; protein-glutamine gamma-glutamyltransferase activity

Biological Process: apoptotic cell clearance; elevation of mitochondrial calcium ion concentration; G-protein signaling, coupled to IP3 second messenger (phospholipase C activating); peptide cross-linking; positive regulation of apoptosis; positive regulation of cell adhesion; reduction of endoplasmic reticulum calcium ion concentration