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Product criteria
| Neuronal TGase (TG6) ELISA |
| Celiac disease antigens |
| Deamidated gliadin peptides |
| Further products for CD research |
| Non-CD antigens |
Product criteria
| Source |
|---|
| E. coli 8 |
| Diagnostics |
| Celiac Disease antigen 4 |
Deamidated gliadin peptides
Detection of gliadin antibodies has been used for a long time in celiac disease diagnostics but suffered from low specificity. This disadvantage was overcome by the introduction of deamidated gliadin peptides as the antigen.
The rationale behind this change 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 of 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 control carrier protein are available (Section: Cereal Proteins).
The rationale behind this change 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 of 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 control carrier protein are available (Section: Cereal Proteins).
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