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. Finally, TGM2 is the autoantigen implicated in celiac disease.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.
Antibody is purified by peptide affinity chromatography method.
Antibody is lyophilized in PBS buffer with 2% sucrose. Add 50 μL of distilled water. Final antibody concentration is 1 mg/mL.
Aliquot and store at -20°C or below. Avoid multiple freeze-thaw cycles.
Type:
Antigen: TGM2
Clonality: Polyclonal
Clone:
Conjugation: Unconjugated
Epitope:
Host: Rabbit
Isotype:
Reactivity: Human
