FDGlcU [Fluorescein di-beta-D-glucuronide]

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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-phrase	H303, H313, H333
Hazard symbol	XN
Intended use	Research Use Only (RUO)
R-phrase	R20, R21, R22
Storage	Freeze (< -15 °C); Minimize light exposure
UNSPSC	12352200

Overview SDS Protocol

Molecular weight

684.55

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

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 mg	0.5 mg	1 mg	5 mg	10 mg
1 mM	146.081 µL	730.407 µL	1.461 mL	7.304 mL	14.608 mL
5 mM	29.216 µL	146.081 µL	292.163 µL	1.461 mL	2.922 mL
10 mM	14.608 µL	73.041 µL	146.081 µL	730.407 µL	1.461 mL

Molarity calculator

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Spectrum

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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

Images

Figure 1. Chemical structure for FDGlcU [Fluorescein di-beta-D-glucuronide]

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)

Histone deacetylase inhibitor FR901228 enhances the antitumor effect of telomerase-specific replication-selective adenoviral agent OBP-301 in human lung cancer cells
Authors: Watanabe T, Hioki M, Fujiwara T, Nishizaki M, Kagawa S, Taki M, Kishimoto H, Endo Y, Urata Y, Tanaka N.
Journal: Exp Cell Res (2006): 256

Induction of apoptosis and inhibition of telomerase activity by trichostatin A, a histone deacetylase inhibitor, in human leukemic U937 cells
Authors: Woo HJ, Lee SJ, Choi BT, Park YM, Choi YH.
Journal: Exp Mol Pathol. (2006)

Enhanced transgene expression in urothelial cancer gene therapy with histone deacetylase inhibitor Okegawa T, Nutahara K, Pong RC, Higashihara E, Hsieh JT. Department of Urology, University of Kyorin, Tokyo, Japan
Authors: Hsieh JT., undefined
Journal: Urol Oncol (2006): 565

Fetal hemoglobin induction by histone deacetylase inhibitors involves generation of reactive oxygen species
Authors: Hsiao CH, Li W, Lou TF, Baliga BS, Pace BS.
Journal: Exp Hematol (2006): 264

DNA damage promotes histone deacetylase 4 nuclear localization and repression of G2/M promoters, via p53 C-terminal lysines
Authors: Basile V, Mantovani R, Imbriano C.
Journal: J Biol Chem (2006): 2347

Real-time gene expression analysis in human xenografts for evaluation of histone deacetylase inhibitors
Authors: Belien A, De Schepper S, Floren W, Janssens B, Marien A, King P, Van Dun J, Andries L, Voeten J, Bijnens L, Janicot M, Arts J.
Journal: Mol Cancer Ther (2006): 2317

Arabidopsis thaliana histone deacetylase 1 (AtHD1) is localized in euchromatic regions and demonstrates histone deacetylase activity in vitro
Authors: Fong PM, Tian L, Chen ZJ.
Journal: Cell Res (2006): 479

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

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