Wheat Gliadin IgG ELISA Kit (DEIA274)

Regulatory status: For research use only, not for use in diagnostic procedures.

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serum, plasma
Species Reactivity
Intended Use
The Gliadin IgG Antibody ELISA Test Kit has been designed for the the detection
and the quantitative determination of specific IgG antibodies against Gliadin in serum and plasma. Further applications in other body fluids are possible and can be requested from the Technical Service. This assay is intended forin-vitro diagnostic use only.
Contents of Kit
1. Microtiter Strips: 96 wells
2. Calibrator A (Negative Control): 2 mL
3. Calibrator B (Cut-Off Standard): 2 mL
4. Calibrator C (Weak Positive Control): 2 mL
5. Calibrator D (Positive Control): 2 mL
6. Enzyme Conjugate: 15 mL
7. Substrate: 15 mL
8. Stop Solution: 15 mL
9. Washing Buffer: 60 mL
For more detailed information, please download the following document on our website.


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Understanding the role of gluten subunits (LMW, HMW glutenins and gliadin) in the networking behavior of a weak soft wheat dough and a strong semolina wheat flour dough and the relationship with linear and non-linear rheology


Authors: Bonilla, Jose C.; Erturk, Merve Y.; Kokini, Jozef L.

The differences in viscoelastic properties of gluten from two very different wheat flours, a weak soft flour dough and a strong semolina dough, primarily caused by their gliadin and glutenin content including gliadin to glutenin ratio were studied. The doughs were subjected to oscillatory time sweep tests at small and large amplitudes as well as small and large frequencies. The gluten subunits (LMW, HMW glutenins and gliadins) tagged with specific fluorescent quantum dots with a distint excitation wavelength were imaged with confocal laser scanning microscopy and their distribution and interactions were measured. The quantitative imaging data was converted into networking data that included lacunarity, network area, and number of network junctions. This networking data was correlated with rheology. The two different dough systems showed different oscillatory behavior during time sweeps. The critical role of LMW glutenins in keeping the structural integrity of semolina doughs was demonstrated by a direct correlation between the non-linear elastic component 'e(3)/e(1)' of the dough and protein network parameters of LMW glutenins. It was also shown that gliadins and HMW glutenins co-localize and associate throughout rheological deformations of the dough. The disruption of the three gluten subunits are responsible for rheological breakdown of soft wheat flour dough, with gliadins influencing the breakdown of the network at higher amplitude deformations. This research presents a new method to analyze the microstructure of wheat doughs and new understanding of how the network structure of the dough subunits contribute and are correlated with fundamental rheological tests.

Identification of Isopeptides Between Human Tissue Transglutaminase and Wheat, Rye, and Barley Gluten Peptides


Authors: Lexhaller, Barbara; Ludwig, Christina; Scherf, Katharina Anne

Celiac disease (CD) is a chronic immune-mediated enteropathy of the small intestine, which is triggered by the ingestion of storage proteins (gluten) from wheat, rye, and barley in genetically predisposed individuals. Human tissue transglutaminase (TG2) plays a central role in the pathogenesis of CD, because it is responsible for specific gluten peptide deamidation and covalent crosslinking, resulting in the formation of N-epsilon-(gamma-glutamyl)-lysine isopeptide bonds. The resulting TG2-gluten peptide complexes are assumed to cause the secretion of anti-TG2 autoantibodies, but the underlying mechanisms are only partly known. To gain more insight into the structures of these complexes, the aim of our study was to identify TG2-gluten isopeptides. With the use of discovery-driven as well as targeted nanoscale liquid chromatography tandem mass spectrometry, we detected 29 TG2-gluten isopeptides in total, involving seven selected TG2 lysine residues (K205, K265, K429, K468, K590, K600, K677). Several gluten peptides carried known B-cell epitopes and/or T-cell epitopes, either intact 9-mer core regions or partial sequences, as well as sequences bearing striking similarities to already known epitopes. These novel insights into the molecular structures of TG2-gluten peptide complexes may help clarify their physiological relevance in the initiation of CD autoimmunity and the role of anti-TG2 autoantibodies.

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