69125
Resorufin methyl ether
suitable for fluorescence, ≥98.0% (HPLC)
Sinónimos:
7-Methoxy-3H-phenoxazin-3-one, Methoxyresorufin, O7-Methylresorufin
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Acerca de este artículo
Fórmula empírica (notación de Hill):
C13H9NO3
Número CAS:
Peso molecular:
227.22
PubChem Substance ID:
UNSPSC Code:
12352200
Beilstein/REAXYS Number:
209529
MDL number:
assay
≥98.0% (HPLC)
form
crystals
mp
≥220 °C (lit.)
solubility
DMF: soluble, DMSO: soluble, alcohols: soluble
fluorescence
λex 571 nm; λem 585 nm in dealkylase(lit.)
suitability
suitable for fluorescence
storage temp.
2-8°C
SMILES string
COc1ccc2N=C3C=CC(=O)C=C3Oc2c1
InChI
1S/C13H9NO3/c1-16-9-3-5-11-13(7-9)17-12-6-8(15)2-4-10(12)14-11/h2-7H,1H3
InChI key
KNYYMGDYROYBRE-UHFFFAOYSA-N
Application
Used to differentiate isozymes of cytochrome P-450
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Clase de almacenamiento
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Xiaowei Zhang et al.
Toxicology and applied pharmacology, 234(3), 306-313 (2008-12-02)
As part of an ongoing effort to understand aryl hydrocarbon receptor (AhR) mediated toxicity in mink, cDNAs encoding for CYP1A1 and the CYP1A2 mixed function monooxygenases were cloned and characterized. In addition, the effects of selected dibenzofurans on the expression
Nicholas E Hadjokas et al.
British journal of pharmacology, 136(3), 347-352 (2002-05-25)
1. Cytochrome P4501A2 (CYP1A2) activates a large number of procarcinogens to carcinogens. Phytochemicals such as flavones can inhibit CYP1A2 activity competitively, and hydroxylated derivatives of flavone (galangin) may be potent, selective inhibitors of CYP1A2 activity relative to CYP1A1 activity. Molecular
A G Krainev et al.
Archives of biochemistry and biophysics, 298(1), 198-203 (1992-10-01)
Some eukaryotic cytochromes P450 (P450s) have a series of ionic amino acids, corresponding to Lys250, Arg251, and Lys253 residues in the P450 1A2 sequence. To understand the roles of those ionic amino acids in the catalytic function of P450, three