Tetramethylbenzidine tmb

Manufactured by BioLegend

Sourced in United States

Tetramethylbenzidine (TMB) is a chromogenic substrate commonly used in enzyme-linked immunosorbent assay (ELISA) and other colorimetric detection applications. It serves as a substrate for horseradish peroxidase (HRP), producing a blue color upon oxidation. The intensity of the color change is proportional to the amount of the target analyte present in the sample.

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Lab products found in correlation

Skanit software, by Thermo Fisher Scientific (1 mentions) Horseradish peroxidase hrp conjugated streptavidin, by BioLegend (1 mentions) Tween 20, by Merck Group (1 mentions) Multiskan go microplate spectrophotometer, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

TMB (16 citations) 3,3′,5,5′-tetramethylbenzidine (TMB) substrate (10 citations) Tetramethylbenzidine (5 citations) Tetramethylbenzidine (TMB) substrate (5 citations) 3,3′,5,5 -tetramethylbenzidine (TMB) substrate set (2 citations)

2 protocols using tetramethylbenzidine tmb

Lectin-Binding Assay for Glycan Detection

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The adjusted serum volume was diluted in PBS and coated in MaxiSorp 96-well Nunc plates under stirring at RT for 2 h. Wells were washed five times in PBS containing 0.05% of Tween 20 (Sigma-Aldrich, St. Louis, MI, USA). Subsequently, 100 µL of biotinylated lectins at an optimised concentration (Table 4) were added inside wells under stirring at RT for 1 h. After washing five times, 0.16 µg/mL of horseradish peroxidase (HRP)-conjugated streptavidin (Biolegend, San Diego, CA, USA) was added for 30 min at RT under stirring. After five washes, a coloured reaction was created using tetramethylbenzidine (TMB; Biolegend, San Diego, CA, USA) and stopped with an 11% sulfuric acid solution. The optical density (OD) was determined at 450 nm with a Multiskan GO microplate spectrophotometer and SkanIt software (Thermo Scientific, Waltham, MA, USA).

Morel M., Pochard P., Echchih W., Dueymes M., Bagacean C., Jousse-Joulin S., Devauchelle-Pensec V., Cornec D., Jamin C., Pers J.O, & Bordron A. (2022). Abnormal B cell glycosylation in autoimmunity: A new potential treatment strategy. Frontiers in Immunology, 13, 975963.

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Quantifying Anti-Env Antibody Reactivity

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50 ng/well of purified Env protein was adsorbed onto 96-well polystyrene plates in 0.1 M bicarbonate (pH 9.6) buffer overnight, washed in phosphate-buffered saline with 0.05% Tween, and blocked in 2% bovine serum albumin (BSA) in phosphate-buffered saline for 2 h. Control wells lacked Env protein, but were blocked the same way. Serum or plasma was added at 0.5% in blocking buffer (with BSA) for 2 h at 4°C, washed extensively, and then incubated with 1:2,000 dilution of horse radish peroxidase-conjugated anti-human IgG. The reaction was then washed, and developed with 3,3’,5,5’-tetra-methylbenzidine (TMB, BioLegend), with the color reaction terminated with 2N sulfuric acid, and the absorbance measured at 450 nm using a plate reader. A dilution series of serum from a selected rheumatoid arthritis patient with high anti-Env reactivity was included on every plate to ensure consistency between plates. The reactivity of this standard (at the same dilution as test samples) was designated as 100 U/ml and all other samples normalised accordingly.

Germon P., Ray M.C., Vianney A, & Lazzaroni J.C. (2001). Energy-Dependent Conformational Change in the TolA Protein of Escherichia coli Involves Its N-Terminal Domain, TolQ, and TolR. Journal of Bacteriology, 183(14), 4110-4114.

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