Coomassie brilliant blue

Manufactured by GenScript

Sourced in United States

Coomassie Brilliant Blue is a dye used for protein detection and quantification. It binds to proteins and produces a blue color, allowing visualization and measurement of protein content in samples.

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Lab products found in correlation

Bis tris protein gel, by Thermo Fisher Scientific (3 mentions) Lithium dodecyl sulfate (lds), by Thermo Fisher Scientific (3 mentions) Ds 11 fx spectrophotometer, by DeNovix (2 mentions)

3 protocols using coomassie brilliant blue

Protein Denaturation and Separation

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All proteins were heated to 95 °C for 5 min under reducing conditions in 1X LDS (Thermo Fisher Scientific, Waltham, MA, USA) and were separated using 4–12% Bis-Tris protein gels (Thermo Fisher Scientific, Waltham, MA, USA). Gels were stained with Coomassie Brilliant Blue (GenScript, Piscataway, NJ, USA). Protein concentrations were determined using the Nanodrop ND-1000 spectrophotometer adjusted by the molar extinction coefficient.

Williams A.E., Shrivastava G., Gittis A.G., Ganesan S., Martin-Martin I., Valenzuela Leon P.C., Olson K.E, & Calvo E. (2021). Aedes aegypti Piwi4 Structural Features Are Necessary for RNA Binding and Nuclear Localization. International Journal of Molecular Sciences, 22(23), 12733.

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Protein Separation and Quantification

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All proteins were heated to 95 °C for 5-10 min under reducing conditions in 1X LDS (Thermo Fisher Scientific, Waltham, MA, USA) and were separated using 4-12% Bis-Tris protein gels (Thermo Fisher Scientific, Waltham, MA, USA). Gels were stained with Coomassie Brilliant Blue (GenScript, Piscataway, NJ, USA). Protein concentrations were determined using the DeNovix DS-11 FX+ spectrophotometer (DeNovix, Wilmington, DE, USA) adjusted by the molar extinction coefficient (MEC; 138200, 136710, 127200 M -1 cm -1 for AeGluc, AnGluc, and CxGluc, respectively).

Williams A.E., Gittis A.G., Botello K., Cruz P., Martin-Martin I., Valenzuela Leon P.C., Sumner B., Bonilla B, & Calvo E. (2024). Structural and functional comparisons of salivary α-glucosidases from the mosquito vectors Aedes aegypti, Anopheles gambiae, and Culex quinquefasciatus. Insect biochemistry and molecular biology, 167.

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Protein SDS-PAGE Quantification Protocol

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All proteins were heated to 95 °C for 5-10 min under reducing conditions in 1X LDS (Thermo Fisher Scientific, Waltham, MA, USA) and were separated using 4-12% Bis-Tris protein gels (Thermo Fisher Scientific, Waltham, MA, USA). Gels were stained with Coomassie Brilliant Blue (GenScript, Piscataway, NJ, USA). Protein concentrations were determined using the DeNovix DS-11 FX+ spectrophotometer (DeNovix, Wilmington, DE, USA) adjusted by the molar extinction coefficient (MEC; 138200, 136710, 127200 M⁻¹ cm⁻¹ for AeGluc, AnGluc, and CxGluc, respectively).

Morando L., Cesa R., Rasetti R., Harvey R, & Strata P. (2001). Role of glutamate δ-2 receptors in activity-dependent competition between heterologous afferent fibers. Proceedings of the National Academy of Sciences of the United States of America, 98(17), 9954-9959.

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