Ridascreen gliadin

Manufactured by R-Biopharm

Sourced in Germany, Austria

The Ridascreen Gliadin is a quantitative enzyme-linked immunosorbent assay (ELISA) test kit used for the detection of gliadin, a component of the gluten protein, in food samples. The kit provides a reliable and accurate method for the analysis of gluten content in various food products.

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Lab products found in correlation

Agraquant gluten g12, by Romer Labs (3 mentions) Ridascreen, by R-Biopharm (1 mentions) Varioskan lux microplate reader, by Thermo Fisher Scientific (1 mentions) Bradford reagent, by Merck Group (1 mentions) Elx808, by Agilent Technologies (1 mentions)

8 protocols using ridascreen gliadin

Sandwich ELISA for Gliadin Quantification

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The same set of samples were analyzed by sandwich ELISA using the Ridascreen Gliadin (R-Biopharm, Darmstadt, Germany). The analytical protocols provided by the kit manufacturer were strictly followed. Each of the samples was extracted and measured in duplicate on a single ELISA plate alongside the supplied standards (representing a gluten concentration of 5–80 mg/kg). The data analyses were performed using Microsoft Excel and Graphpad Prism. The results of absorbance readings were analyzed according to the kit manufacturer’s instructions using cubic polynomial regression for the standard curve.

Li H., Bose U., Stockwell S., Howitt C.A, & Colgrave M. (2019). Assessing the Utility of Multiplexed Liquid Chromatography-Mass Spectrometry for Gluten Detection in Australian Breakfast Food Products. Molecules, 24(20), 3665.

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Sandwich ELISA Detection of Gluten

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Sandwich enzyme-linked immunosorbent assays (ELISAs) were carried out employing the R5 monoclonal antibody (RIDA-SCREEN Gliadin, R-Biopharm, Darmstadt, Germany) and G12 monoclonal antibody (AgraQuant ELISA Gluten G12, Romer Labs, Union, MO). The R5 and G12 ELISA assays have detection limits of 3 and 2 ppm for gluten, respectively. Experiments were performed according to the manufacturer’s instructions.
For the R5 ELISA, samples were diluted 1:1,000-fold with dilution buffer. Aliquots of 100 μl were added to the R5-coated microtiter plate. The plates were incubated for 30 min at room temperature, washed, and incubated with 100 μl of peroxidase-conjugated secondary antibody for 30 min at room temperature. After washing, substrate solution containing tetramethylbenzidine was added, followed by the addition of 100 μl stop reagent. After 30 min, the absorbance was measured at 450 nm. For the G12 ELISA, samples were diluted 1:300-fold in dilution buffer and 100 μl aliquots were added to the G12-coated microtiter plate. After incubation for 20 min, plates were washed, 100 μl of the conjugate was added for 20 min, followed by substrate solution for 20 min, addition of 100 μl stop solution, and measurement of the absorbance at 450 nm.

Wei G., Tian N., Valery A.C., Zhong Y., Schuppan D, & Helmerhorst E.J. (2015). Identification of Pseudolysin (lasB) as an Aciduric Gluten-Degrading Enzyme with High Therapeutic Potential for Celiac Disease. The American journal of gastroenterology, 110(6), 899-908.

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Gliadin Content Assessment in Hydrolysates

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In hydrolysates obtained by one- and two-step hydrolysis, gliadin content was assessed by immunoenzymatic assay with G12 (AgraQuant^® Gluten G12^®; Romer Labs GmbH, Tulln an der Donau, Austria) and R5 (RIDASCREEN^® Gliadin; R-Biopharm Inc., Pfungstadt, Germany) antibodies according to the manufacturer’s instructions and previous report [5 (link)]. The G12 monoclonal antibody recognizes an immunoreactive 33-mer peptide, while the R5 monoclonal antibody recognizes a potentially immunogenetic QQPFP sequence that occurs multiple times in prolamine molecules. Assays were performed in triplicate, and gliadin content was calculated based on the standard curve. The results are presented as relative residual immunoreactivity [%] in respect to the untreated gliadin sample or prehydrolyzed gliadin by commercial digestive enzymes in the case of two-step hydrolysis.

Leszczyńska J., Szczepankowska A.K., Majak I., Mańkowska D., Smolińska B., Ścieszka S., Diowksz A., Cukrowska B, & Aleksandrzak-Piekarczyk T. (2024). Reducing Immunoreactivity of Gluten Peptides by Probiotic Lactic Acid Bacteria for Dietary Management of Gluten-Related Diseases. Nutrients, 16(7), 976.

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Gluten-Free Bread Gluten Analysis

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To ensure the gluten content remained below the required threshold (<3 ppm), gluten analysis was conducted on the prepared bread. To accurately measure gluten levels, specialized testing methods such as Ridascreen Gliadin (R-Biopharm AG, Darmstadt, Germany); Veratox for Gliadin R5 (Neogen, Lansing, Michigan, USA); and AgraQuant Gluten G12 (Romer Labs, Getzersdorf, Austria) were used. All values were designated as mean ± standard deviation (n = 3).
The gluten content in the gluten-free bread product was analyzed using the gliadin test Ridascreen (R-Biopharm AG, Darmstadt, Germany), which was also used by Ja Myung Yu [64 (link)].

Utarova N., Kakimov M., Gajdzik B., Wolniak R., Nurtayeva A., Yeraliyeva S, & Bembenek M. (2024). Development of Gluten-Free Bread Production Technology with Enhanced Nutritional Value in the Context of Kazakhstan. Foods, 13(2), 271.

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Protein and Gluten Quantification in Wheat

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Protein estimations were performed using a Coomassie dye binding protein assay using Bradford reagent (Sigma-Aldrich, St Louis, USA) following the manufacturer's instructions. Measurements were made at 595 nm using a Varioskan LUX microplate reader (Thermo Scientific, Scoresby, Australia). Bovine serum albumin (BSA) standard was used in the linear range 0.125–1.5 mg/mL.
Diluted wheat extracts were analyzed by sandwich ELISA using the Ridascreen Gliadin (R-Biopharm, Darmstadt, Germany). The analytical protocols provided by the kit manufacturer were strictly followed. Each of the samples was extracted using the extraction Cocktail (R7006/R7016, R-Biopharm) recommended by the manufacturer for optimal gluten extraction and measured on the using Varioskan LUX microplate reader (Thermo Scientific) in duplicate on a single ELISA plate alongside the supplied standards (representing a gluten concentration of 5–80 mg/kg). The results of absorbance readings were analyzed according to the kit manufacturer's instructions using cubic polynomial regression for the standard curve. The data analyses were performed using Microsoft Excel.

Nye-Wood M.G., Juhász A., Bose U, & Colgrave M.L. (2021). Proteome Analysis and Epitope Mapping in a Commercial Reduced-Gluten Wheat Product. Frontiers in Nutrition, 8, 705822.

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Gluten Analysis of Food Samples

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Upon arrival at WFSR, the DP were stored at 4°C. Each DP was weighted and then homogenised by grinding or pureeing five times 10 s (Moulinex DP700) or shaking (depending on the type of food) before gluten analysis. The gluten analysis was performed by using the RidaScreen gliadin (R-Biopharm, Art no. R7001) method which is an ELISA sandwich method, based on the R5 antibody, currently recommended by Codex Alimentarius (15) . The test was performed following the instructions in the user manual, except for the sample volume that was increased to 1 g, keeping the sample:extraction buffer ratio constant, and applying UPEX extraction buffer as described by Mena et al. (16) to increase the accuracy of the method, with similar detected gluten levels (in house comparison, data not shown). Per DP, one sample was extracted and divided over two wells to be tested. During the test, a colour signal was produced which was measured at the absorbance wavelength of 450 nm in a spectrophotometer (Biotek ELx808). The signals of the two wells were averaged and compared with a standard curve of known gluten concentrations (standard curve is shown in online Supplementary Fig. S1). In this way, the gluten concentration was determined in each sample.

van der Fels-Klerx H.J., Smits N.G.E., Bremer M.G.E.G., Schultink J.M., Nijkamp M.M., Castenmiller J.J.M, & de Vries J.H.M. (2021). Detection of gluten in duplicate portions to determine gluten intake of coeliac disease patients on a gluten-free diet. The British journal of nutrition, 125(9).

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Comparative Evaluation of ELISA Kits for Gluten Detection

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The four spiked samples
were analyzed using four ELISA systems, including Ridascreen Gliadin
(“R5”, R7001, R-Biopharm), AgraQuant gluten G12 (Romer-Labs, Austria), Ridascreen Total Gluten (R7041, R-Biopharm, Germany), and Wheat/Gluten ELISA kit II (Morinaga, Japan). Table 1 summaries the details of each ELISA kit. Total hordein
isolate served as a common external hordein standard for all kits.
Three individual extractions of each spiking level were conducted,
and three measurements of each extraction were performed. Two sets
of kit standards and two sets of hordein external standards were also
served. The recovery was calculated by dividing the calibrated gluten
content results with the theoretical spiking hordein content.

Huang X., Ahola H., Daly M., Nitride C., Mills E.C, & Sontag-Strohm T. (2022). Quantification of Barley Contaminants in Gluten-Free Oats by Four Gluten ELISA Kits. Journal of Agricultural and Food Chemistry, 70(7), 2366-2373.

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Collaborative Validation of Gluten-Free Food Analysis

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Following the AOAC guidelines, which are published as Appendix D (11 ) and Appendix M (12 ), an international collaborative study was set up to validate the RIDASCREEN Gliadin for additional matrixes from important gluten-free food categories as an extension of AOAC Official Method 2012.01. The experiment consisted of 32 different samples (19 different matrixes from 16 different food categories) that were analyzed as duplicates in a blinded manner. To allow a uniform calculation of results later, participants were advised to deliver raw OD data by a data return sheet. The study director did the calculation of results using the curve fitting procedure mentioned in the test kit insert of the RIDASCREEN Gliadin (R7001, R-Biopharm).

Lacorn M., Dubois T., Weiss T., Zimmermann L., Schinabeck T.M., Loos-Theisen S, & Scherf K. (2021). Determination of Gliadin as a Measure of Gluten in Food by R5 Sandwich ELISA RIDASCREEN® Gliadin Matrix Extension: Collaborative Study 2012.01. Journal of AOAC International, 105(2), 442-455.

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