B4651
3-Bromo-3-methyl-2-(2-nitrophenylthio)-3H-indole
≥85%
Synonym(s):
2-(2-Nitrophenylsulfenyl)-3-methyl-3-bromoindolenine, 3-Bromo-3-methyl-2-(2-nitrophenylmercapto)-3H-indole, BNPS-skatol
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About This Item
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Assay
≥85%
storage temp.
−20°C
SMILES string
CC1(Br)C(Sc2ccccc2[N+]([O-])=O)=Nc3ccccc13
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
InChI key
BXTVQNYQYUTQAZ-UHFFFAOYSA-N
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Application
Peptide cleavage reagent specific for the carboxyl side of tryptophan residues.
Storage Class Code
13 - Non Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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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
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
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
The core domain of hirudin from the leech Hirudinaria manillensis. Chemical modification of a tryptophan-containing synthetic peptide analog.
Advances in experimental medicine and biology, 398, 627-633 (1996-01-01)
Biochemistry and cell biology = Biochimie et biologie cellulaire, 75(6), 709-715 (1997-01-01)
A concerted conformational change in Bacillus subtilis tryptophanyl-tRNA synthetase (TrpRS) was evident from previous fluorescence on the quenching of the single Trp residue Trp-92 in the 4FTrp-AMP complexed enzyme. In this study, chemical modifications of the B. subtilis TrpRS were
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