tTG is a critical enzyme involved in tissue repair within the small intestine. When individuals with celiac disease consume gluten, their immune systems produce antibodies against tTG, initiating an autoimmune response that damages the intestinal lining. tTG neo represents a modified form of this enzyme, which reacts more precisely with gluten-induced changes in the tissue, allowing for greater diagnostic specificity.

Research shows that tTG antibodies are highly specific and sensitive markers for celiac disease, providing essential insight into the immune response associated with gluten ingestion. The addition of tTG neo allows early detection of immune reactions that might otherwise go unnoticed with conventional tTG testing, especially in early-stage or atypical presentations.

Microbial transglutaminase is an enzyme commonly added to processed foods, including gluten-free products like dairy and plant-based meat alternatives, to enhance texture and shelf life.

Due to its enzymatic similarity to human tissue transglutaminase (tTG), microbial transglutaminase (mTG) can cross-link protein structures, forming complexes (mTG neo-epitopes) that exhibit cross-reactivity with those generated by tTG and gliadin peptides (tTG neo-epitopes). Antibodies against these mTG neo-epitopes can be specifically detected in patients with non-celiac gluten sensitivity (NCGS) and celiac disease. Recent studies indicate that NCGS patients often exhibit detectable antibodies against pure mTG. Therefore, the additional detection of anti-mTG antibodies serves as a valuable diagnostic tool for identifying NCGS. This marker broadens the diagnostic scope for gluten sensitivity by addressing a possible hidden immune trigger. Studies show that mTG can stimulate immune responses similar to tTG, suggesting its role in immune activation in NCGS and celiac-related symptoms. Ongoing research into antibodies against mTG and mTG neo aims to improve understanding and management of gluten-related disorders, especially when symptoms persist on a gluten-free diet.

Deamidated Gliadin Peptides are modified gluten fragments that elicit a strong immune response, making DGP antibodies a highly specific marker for gluten-related disorders. DGP testing is especially useful for diagnosing celiac disease, as DGP antibodies (particularly the IgA and IgG isotypes) demonstrate high sensitivity and specificity. This makes DGP valuable in identifying patients with mild or “silent” presentations of celiac disease, often detecting cases that traditional markers, like anti-tTG and anti-endomysial antibodies (EmA), may miss.

DGP testing also provides a reliable way to monitor adherence to a gluten-free diet (GFD), as antibody levels typically decrease with strict dietary compliance. By incorporating DGP antibodies into diagnostic protocols, healthcare professionals can identify subtle immune responses to gluten and effectively monitor patient compliance with a GFD, offering comprehensive support in managing celiac disease and gluten sensitivities.

Gliadin is a prolamin protein in wheat gluten, rich in proline and glutamine residues, making it resistant to complete digestion by gastrointestinal enzymes. This resistance leads to the formation of peptides that can cross the intestinal barrier and interact with the immune system. Frazer's Fraction refers to a specific subset of these gliadin peptides that have been identified as highly immunogenic, meaning they are particularly effective at triggering immune responses. These peptides are recognized by T-cells in individuals with celiac disease, leading to inflammation and damage to the intestinal mucosa. The identification of Frazer's Fraction has been instrumental in understanding the pathogenesis of celiac disease and has implications for developing targeted diagnostic tests and therapies.

Testing for TG3 antibodies is a critical tool in diagnosing certain types of GRDs, particularly for individuals with atypical or skin-specific symptoms related to gluten exposure. In patients with dermatitis herpetiformis, TG3 antibodies are highly specific and help confirm the presence of celiac disease even when gastrointestinal symptoms are absent. Detecting TG3 antibodies supports accurate diagnosis, improves patient outcomes, and allows for personalized treatment plans, such as strict gluten elimination, which can mitigate symptoms and prevent further immune-mediated damage.