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About This Item
Empirical Formula (Hill Notation):
C15H11BrN2O2S
CAS Number:
Molecular Weight:
363.23
EC Number:
248-737-9
UNSPSC Code:
12352200
PubChem Substance ID:
Beilstein/REAXYS Number:
1491457
MDL number:
InChI key
BXTVQNYQYUTQAZ-UHFFFAOYSA-N
InChI
1S/C15H11BrN2O2S/c1-15(16)10-6-2-3-7-11(10)17-14(15)21-13-9-5-4-8-12(13)18(19)20/h2-9H,1H3
SMILES string
CC1(Br)C(Sc2ccccc2[N+]([O-])=O)=Nc3ccccc13
assay
≥85%
storage temp.
−20°C
Application
Peptide cleavage reagent specific for the carboxyl side of tryptophan residues.
Storage Class
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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J E Moskaitis et al.
Neurochemical research, 11(2), 299-315 (1986-02-01)
The interactions of sodium dodecyl sulfate with a number of proteins were examined at a variety of pH values ranging from 4.8 to 11.6. The dodecyl sulfate-induced precipitation of some of these proteins was observed within a relatively limited range
V Rahali et al.
Journal of protein chemistry, 18(1), 1-12 (1999-03-11)
A comparative study of various procedures for tryptophanyl peptide bond cleavage by BNPS-skatole [2-(2-nitrophenyl)-3-methyl-3-bromoindolenine] was carried out on native and on reduced and alkylated bovine beta-lactoglobulin (BLG). The reaction yield and the composition of the derived products were studied in
Hee-Kyoung Lee et al.
Biochemical and biophysical research communications, 315(1), 1-9 (2004-03-12)
Squalene epoxidase (SE) catalyzes the conversion of squalene to (3S)-2,3-oxidosqualene. Photolabeling and site-directed mutagenesis were performed on recombinant rat SE (rrSE) in order to identify the location of the substrate-binding site and the roles of key residues in catalysis. Truncated
V Rahali et al.
Die Nahrung, 44(2), 89-95 (2000-05-05)
Bovine beta-Lactoglobulin (BLG) was cleaved by BNPS-skatole (2-(2'-nitrophenylsulfenyl)-3-methyl-3'-bromoindolenine), trypsin, or pepsin in 40% ethanol before emulsification with hexadecane in order to characterize the peptides active at the interfaces. The total digests and the different phases obtained after emulsification were analyzed
N Swamy et al.
Archives of biochemistry and biophysics, 373(2), 471-478 (2000-01-06)
The multiple physiological properties of vitamin D-binding protein (DBP) include organ-specific transportation of vitamin D(3) and its metabolites, manifested by its ability to bind vitamin D sterols with high affinity. In the present investigation we probed the vitamin D sterol-binding
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