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SML4017

Sigma-Aldrich

DiFMU

new

≥98% (HPLC)

Synonym(s):

6,8-Difluoro-7-hydroxy-4-methyl-2H-1-benzopyran-2-one, 6,8-Difluoro-7-hydroxy-4-methylcoumarin, Marina Blue

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About This Item

Empirical Formula (Hill Notation):
C10H6F2O3
CAS Number:
215868-23-8
Molecular Weight:
212.15
MDL number:
MFCD01073675
UNSPSC Code:
12352200

Quality Level

100

Assay

≥98% (HPLC)

form

powder

color

white to beige

solubility

DMSO: 2 mg/mL, clear

storage temp.

2-8°C

SMILES string

FC1=C2C(C(C)=CC(O2)=O)=CC(F)=C1O

Biochem/physiol Actions

Fluorescent product of hydrolysis of fluorogenic phosphatase substrate DiFMUP.



DiFMU is a fluorescent product of hydrolysis of fluorogenic phosphatase substrate DiFMUP. DiFMU excitation wavelength is 358nm and emission can be detected at 455 nm.

Pictograms

Skull and crossbones
GHS06

Signal Word

Danger

Hazard Statements

H301,H317

Hazard Classifications

Acute Tox. 3 Oral - Skin Sens. 1

Storage Class Code

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Yue Ge et al.
Analytical biochemistry, 362(1), 63-68 (2007-01-24)
We describe a fluorescence-based assay for the analysis of xylanase activity using a novel fluorogenic substrate, 6,8-difluoro-4-methylumbelliferyl beta-D-xylobioside (DiFMUX(2)). Generation of fluorescent 6,8-difluoro-4-methylumbelliferone (DiFMU) from the substrate corresponded directly to xylanase activity. High-performance liquid chromatography analysis of the digestion products
Lei Sun et al.
Biomolecules, 5(3), 1284-1301 (2015-07-02)
Protein phosphatase 2A (PP2A) is one of the most abundant intracellular serine/threonine (Ser/Thr) phosphatases accounting for 1% of the total cellular protein content. PP2A is comprised of a heterodimeric core enzyme and a substrate-specific regulatory subunit. Potentially, at least seventy
Stefan Welte et al.
Analytical biochemistry, 338(1), 32-38 (2005-02-15)
The fluorogenic substrate 6,8-difluoro-4-methylumbiliferyl phosphate (DIFMUP) has been widely used for the detection of serine and threonine phosphatase activities. Here we describe the use of this substrate for the characterization of protein tyrosine phosphatases (PTPs) and for the screening for

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