Transglutaminase Antibody Iga

Description: 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. TGM2 acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. It has been identified as the autoantigen implicated in celiac disease.

Description: 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. TGM2 acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. It has been identified as the autoantigen implicated in celiac disease.

Description: 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. TGM2 acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. It has been identified as the autoantigen implicated in celiac disease.

Description: 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. TGM2 acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. It has been identified as the autoantigen implicated in celiac disease.

Description: Additional name(s) for this target protein: TGM3, TG3

Description: Additional name(s) for this target protein: TG4; TGM4

Description: Transglutaminase 2, also called TGC, TG2 and TGM2, is a 78-kDa, calcium dependent enzyme of the protein-glutamine gamma-glutamyltransferases family. Transglutaminases (TGs) are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of TGs are not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. Transglutaminase 2 acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. It is the autoantigen implicated in celiac disease.

Description: Transglutaminase 2, also called TGC, TG2 and TGM2, is a 78-kDa, calcium dependent enzyme of the protein-glutamine gamma-glutamyltransferases family. Transglutaminases (TGs) are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of TGs are not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. Transglutaminase 2 acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. It is the autoantigen implicated in celiac disease.

Description: Additional name(s) for this target protein: Transglutaminase 6; Tgm6; Tg6

Description: Additional name(s) for this target protein: TGM2; TG2

Description: Recognizes a 77-85kDa protein, identified as cellular or tissue transglutaminase II (TGase II). 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. The identification of transglutaminase as the main antigen of endomysium antibodies allows a new diagnostic approach to celiac disease (CD), a genetic, immunologically mediated small bowel enteropathy that causes malabsorption. TGase II is implicated in programmed cell death, signal transduction, drug-resistance, cell growth, endocytosis, insulin secretion, cell adhesion, cataract formation, and wound healing.

Description: Recognizes a 77-85kDa protein, identified as cellular or tissue transglutaminase II (TGase II). 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. The identification of transglutaminase as the main antigen of endomysium antibodies allows a new diagnostic approach to celiac disease (CD), a genetic, immunologically mediated small bowel enteropathy that causes malabsorption. TGase II is implicated in programmed cell death, signal transduction, drug-resistance, cell growth, endocytosis, insulin secretion, cell adhesion, cataract formation, and wound healing.