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Fluorescent Dyes  >  Enzyme Detection Reagents  >>  Resorufin β-D-Galactopyranoside

Product Name Resorufin β - D - Galactopyranoside
Size 25 mg
Catalog # AS-85617
US$ $93
Description

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. This substrate is especially useful for sensitive enzyme measurements in ELISAs. 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.

Minimum Purity: 95%

Detailed Information Material Safety Data Sheets (MSDS)
Storage -20C desiccated and protected from light
References Yang NC and Hu ML (2004). A fluorimetric method using fluorescein di-?-D-galactopyranoside for quantifying the senescence-associated ?-galactosidase activity in human foreskin fibroblast Hs68 cells. Anal Biochem 325, 337-43, Chiocconi A, et al. (2000). Synthesis of 4-nitrophenyl ?-D-fucofuranoside and ?-D-fucofuranosyl-(1?3)-D-mannopyranose: modified substrates for studies on catalytic requirements of ?-D-galactofuranosidase. Carbohydr Res 323, 7-13, Hakamata W, et al. (2000). Hydrolytic activity of ?-galactosidases against deoxy derivatives of p-nitrophenyl ?-D-galactopyranoside. Carbohydr Res 324, 107-15, Weiss DJ, et al. (1997). In situ histochemical detection of ?-galactosidase activity in lung: assessment of X-Gal reagent in distinguishing lacZ gene expression and endogenous ?-galactosidase activity. Hum Gene Ther 8, 1545-54, Lukomskaya IS, et al. (1996). Use of ?-maltosides (p-nitrophenyl-?-D-maltoside, 2-chloro-4-nitrophenyl- ?-D-maltoside and 4-methylumbelliferyl-?-D-maltoside) as substrates for the assay of neutral ?-glucosidase from human kidney and urine. Clin Chim Acta 244, 145-54, Usui T, et al. (1992). Enzymatic synthesis of p-nitrophenyl 4(5)-O-?-D-galactosyl-?-maltopentaoside as a substrate for human ?-amylases. Anal Biochem 202, 61-7, Cousin MA, et al. (1989). Detection of ?-galactofuranosidase production by Penicillium and Aspergillus species using 4-nitrophenyl ?-D-galactofuranoside. J Appl Bacteriol 66, 311-7, Bowen DM and Radin NS (1969). Hydrolase activities in brain of
Molecular Weight 375.33
Spectral Properties Abs/Em = 573/585 nm
Solvent System DMSO
     
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