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 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
Enter any two values (mass, volume, concentration) to calculate the third.
Mass (Calculate) | Molecular weight | Volume (Calculate) | Concentration (Calculate) | Moles | ||||
/ | = | x | = |
Spectrum
Open in Advanced Spectrum Viewer
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)
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
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
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
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
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