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.
Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
Target:
The synthetic peptide sequence used to generate the antibody AP7826c was selected from the Center region of human TGM2. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
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