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About This Item
Empirical Formula (Hill Notation):
C9H12BrNO3S
CAS Number:
Molecular Weight:
294.17
NACRES:
NA.22
PubChem Substance ID:
UNSPSC Code:
12352100
EC Number:
249-105-5
MDL number:
Assay:
≥95%
Form:
solid
InChI key
VEGVMTIJKACZGO-UHFFFAOYSA-N
InChI
1S/C9H11NO3S.BrH/c1-14(2)6-7-5-8(10(12)13)3-4-9(7)11;/h3-5H,6H2,1-2H3;1H
SMILES string
[Br-].C[S+](C)Cc1cc(ccc1O)[N+]([O-])=O
assay
≥95%
form
solid
storage temp.
2-8°C
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Gloves
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Y M Peyser et al.
FEBS letters, 259(2), 346-348 (1990-01-01)
Rabbit skeletal muscle myosin subfragment-1 (S-1) was reacted with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide (DHNBS) resulting in modification of 0.8 tryptophan residues per S-1. In order to assign the most reactive tryptophan of the 5 S-1 tryptophans, antibodies were raised in rabbits against
Inactivation of the nucleoside transporter of the human erythrocyte by dimethyl (2-hydroxy-5-nitrobenzyl) sulphonium bromide.
S D Thorne et al.
Biochemical Society transactions, 19(4), 418S-418S (1991-11-01)
Structure-function relationship in the allosteric L-lactate dehydrogenases from Lactobacillus casei and Lactobacillus curvatus.
U Mayr et al.
European journal of biochemistry, 126(3), 549-558 (1982-09-01)
G I Karp et al.
Archives of biochemistry and biophysics, 233(2), 712-720 (1984-09-01)
A single tryptophan residue on antithrombin has been modified with dimethyl-(2-hydroxy-5-nitrobenzyl)sulfonium bromide. This alteration led to a 500-fold reduction in the heparin-dependent acceleration of thrombin-modified antithrombin interactions, as well as a 10-fold decrease in the avidity of the modified protease
J E McLean et al.
Biochemistry, 40(7), 2194-2200 (2001-05-01)
Brequinar and the active metabolite of leflunomide, A77 1726, have been clearly shown to inhibit human dihydroorotate dehydrogenase (DHODH), but conflicting mechanisms for their inhibition have been reported. DHODH catalyses the conversion of dihydroorotate (DHO) to orotate concurrent with the
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