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FDGlcU [Fluorescein di-beta-D-glucuronide]

The beta-glucuronidase (GUS) enzyme from E. coli (EC 3.2.1.31) has been well documented to provide desirable characteristics as a marker gene in transformed plants. The GUS reporter gene system has many advantages including stable expression of E. coli GUS enzyme, no interference with normal plant metabolism, and low intrinsic GUS activity in higher plants. FDGlcU is considered to be one of the most sensitive fluorogenic substrates available for detecting beta-glucuronidase. The colorless and nonfluorescent FDGlcU is hydrolyzed to highly fluorescent fluorescein, which exhibits excellent spectral properties that match the optimal detection window of most fluorescence instruments. Glucuronidase-catalyzed hydrolysis of FDGlcU can be followed by fluorescence increase around 520 nm. Alternatively, FDGlcU can also be used to detect glucuronidase in a chromogenic mode since the enzymatic product (fluorescein) exhibits a large extinction coefficient (close to 100,000 cm-1mol-1). FDGlcU has been used for identifying GUS-positive cells with fluorescence microscopy and flow cytometry.

Calculators

Common stock solution preparation

Table 1. Volume of DMSO needed to reconstitute specific mass of FDGlcU [Fluorescein di-beta-D-glucuronide] to given concentration. Note that volume is only for preparing stock solution. Refer to sample experimental protocol for appropriate experimental/physiological buffers.

0.1 mg0.5 mg1 mg5 mg10 mg
1 mM146.081 µL730.407 µL1.461 mL7.304 mL14.608 mL
5 mM29.216 µL146.081 µL292.163 µL1.461 mL2.922 mL
10 mM14.608 µL73.041 µL146.081 µL730.407 µL1.461 mL

Molarity calculator

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Spectrum

References

View all 80 references: Citation Explorer
Active site tyrosine is essential for amidohydrolase but not for esterase activity of a class 2 histone deacetylase-like bacterial enzyme
Authors: Moreth K, Riester D, Hildmann C, Hempel R, Wegener D, Schober A, Schwienhorst A.
Journal: Biochem J. (2006)
The histone deacetylase inhibitor trichostatin a has genotoxic effects in human lymphoblasts in vitro
Authors: Olaharski AJ, Ji Z, Woo JY, Lim S, Hubbard AE, Zhang L, Smith MT.
Journal: Toxicol Sci (2006): 341
Histone deacetylase (HDAC) 4 involvement in both Lewy and Marinesco bodies
Authors: Takahashi-Fujigasaki J, Fujigasaki H.
Journal: Neuropathol Appl Neurobiol (2006): 562
Experimental therapy of malignant gliomas using the inhibitor of histone deacetylase MS-275
Authors: Eyupoglu IY, Hahnen E, Trankle C, Savaskan NE, Siebzehnrubl FA, Buslei R, Lemke D, Wick W, Fahlbusch R, Blumcke I.
Journal: Mol Cancer Ther (2006): 1248
Role of histone deacetylase Rpd3 in regulating rRNA gene transcription and nucleolar structure in yeast
Authors: Oakes ML, Siddiqi I, French SL, Vu L, Sato M, Aris JP, Beyer AL, Nomura M.
Journal: Mol Cell Biol (2006): 3889
Page updated on July 12, 2023

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Catalog Number14002
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Physical properties

Molecular weight

684.55

Solvent

DMSO

Spectral properties

Absorbance (nm)

487

Correction Factor (260 nm)

0.32

Correction Factor (280 nm)

0.35

Extinction coefficient (cm -1 M -1)

800001

Excitation (nm)

498

Emission (nm)

517

Quantum yield

0.79001, 0.952

Storage, safety and handling

H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22

Storage

Freeze (< -15 °C); Minimize light exposure
UNSPSC12352200
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