Resorufin β-D-galactopyranoside

Product ID: M0203

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  • Buy 5 for $45.40 each and save 20%

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Red fluorogenic substrate for lacZ β-galactosidase activity, intracellularly, or in vitro.

This stable fluorogenic substrate for lacZ β-galactosidase activity, releases resorufin M0202 upon β-galactosidase enzyme cleavage. Unlike FDG that requires a two-step hydrolysis to generate maximum fluorescence, resorufin β-D-galactopyranoside requires only a single-step hydrolysis reaction to attain full fluorescence making it especially useful for sensitive enzyme measurements in applications such as ELISAs or high-content screening (HCS) systems. The relatively low pKa (~6.0) of resorufin (the enzymatic hydrolysis product of resorufin galactoside) with Ex/Em=573/585 nm permits continuous measurement of enzymatic activity. Resorufin galactoside has also been used to quantitate β-galactosidase activity in single yeast cells by flow cytometry and to detect immobilized β-galactosidase activity. Marker Gene produces a high-purity, molecular biology grade of this substrate for your research needs. Ask about the availability of bulk quantities.

Technical Data
SKU M0203
CAS Number 95079-19-9
Unit Size 10mg
Alternative Names 3-Phenoxazone 7-(β-D-galactopyranoside)
Absorption 470nm
Extinction 18
Detection Method Fluorescence
Molecular Formula C₁₈H₁₇NO₈
Molecular Weight 375.33
Soluble In DMSO, H₂O
Storage Conditions -20C, Desiccated, Protect From Light

References and Citations


  • Rodrigue J, Ganne G, Blanchard B, Saucier C, Giguère D, Shiao TC, Varrot A, Imberty A, Roy R. (2013) "Aromatic thioglycoside inhibitors against the virulence factor LecA from Pseudomonas aeruginosa." Org Biomol Chem. 11(40):6906-18.
  • Leclair Ellis J, Tomasko DL, Dehghani F. (2008) "Novel dense CO2 technique for beta-galactosidase immobilization in polystyrene microchannels." Biomacromolecules. 9(3):1027-34.
  • Yates RM, Hermetter A, Taylor GA, Russell DG. (2007) " Macrophage activation downregulates the degradative capacity of the phagosome." Traffic. 8(3):241-50.
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  • Eggertson MJ, Craig DB, (1999) "Beta-galactosidase assay using capillary electrophoresis laser-induced fluorescence detection and resorufin-beta-D-galactopyranoside as substrate." Biomed. Chromatogr. 13: 516-519.
  • Westerfield M, Wegner J, Jegalian BG, DeRobertis EM, Puschel AW (1992) "Specific activation of mammalian Hox promoters in mosaic transgenic zebrafish" Genes & Develop. 6: 591-598.
  • Hadd AG, Raymond DE, Halliwell JW, Jacobson SC, Ramsey JM. (1997) "Microchip device for performing enzyme assays." Anal. Chem. 69: 3407-3412.
  • Jones DE, Cui DM, Miller DM. (1995) "Expression of beta-galactosidase under the control of the human c-myc promoter in transgenic mice is inhibited by mithramycin." Oncogene 10: 2323-2330.
  • Sernetz M, Willems H, Keiner K. (1990) "Dispersive analysis of turnover rates of a CST reactor by flow-through microfluorometry under conditions of growth." Ann. NY Acad. Sci. 613: 333-337.
  • Wittrup KD, Bailey JE (1998) "A single-cell assay of beta-galactosidase activity in Saccharomyces cerevisiae." Cytometry 9: 394.
  • Willems H, Sernetz M. (1998) "Flow fluorimetric investigations on reaction kinetics of a growing analytical bioreactor." Anal. Chim. Acta 213: 245.
  • Hofmann J, Serretz M (1984) "Immobilized enzyme kinetics analyzed by flow-through microfluorimetry. Resorufin-B-D-galactopyranoside as a new fluorogenic substrate for galactosidase." , Anal. Chim. Acta 163: 67.
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