Detection of gliadin antibodies has been used for a long time in celiac disease diagnostics, but suffered from a low specificity. This disadvantage was overcome by the introduction of deamidated gliadin peptides as antigen.
The ratio behind is that tissue transglutaminase catalyzes gliadin deamidation in the intestinal mucosa of celiac disease patients, resulting in deamidated gliadin peptides which are recognized by HLA receptors of immune cells. Therefore, deamidated gliadin antibodies are specific for celiac disease.
We introduced four different variations of deamidated gliadin antigens composed by a carrier protein linked with a combination of the deamidated 33-mer and 26-mer gamma gliadin peptides and the DQ2-GI- and DQ2-GII-peptides (Dørum S. et al., J Proteome Res. 2009; 8:1748-55). In addition, the non-deamidated native versions as well as the carrier protein control are available (Section: Cereal Proteins).