D6388
Dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide
≥95%
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About This Item
Empirical Formula (Hill Notation):
C9H12BrNO3S
CAS Number:
Molecular Weight:
294.17
EC Number:
MDL number:
UNSPSC Code:
12352100
PubChem Substance ID:
NACRES:
NA.22
Recommended Products
Assay
≥95%
form
solid
storage temp.
2-8°C
SMILES string
[Br-].C[S+](C)Cc1cc(ccc1O)[N+]([O-])=O
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
InChI key
VEGVMTIJKACZGO-UHFFFAOYSA-N
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - 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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Heparin binding and protease inhibitor activity of chemically modified antithrombin III.
M N Blackburn et al.
Annals of the New York Academy of Sciences, 370, 700-707 (1981-01-01)
M F Scully et al.
Thrombosis and haemostasis, 65(4), 351-354 (1991-04-08)
Chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNBSB) generates products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl [HNB] incorporated/mole of antithrombin III) but with high or low affinity for heparin-Sepharose. Upon
M M Werber et al.
Biochemistry, 26(10), 2903-2909 (1987-05-19)
Modification of tryptophanyl residues (Trps) of myosin subfragments 1 (S-1) was performed with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide (DHNBS). Under controlled conditions, pH 6 at 0 degrees C and 10-min reaction with 10-100-fold molar excess, K+(EDTA) activity was reduced down to less than
C B Peterson et al.
The Journal of biological chemistry, 262(16), 7552-7558 (1987-06-05)
Heparin has been shown to exhibit lower affinity for the antithrombin-thrombin complex than for antithrombin alone (Carlstrom, A.-S., Lieden, K., and Bjork, I. (1977) Thromb. Res. 11, 785-797), suggesting that structural alterations in antithrombin may accompany its reaction with thrombin.
S Park et al.
Biochemistry, 39(38), 11732-11741 (2000-09-20)
The fluorescence intensity difference between rabbit skeletal myosin subfragment 1 (S1) and nucleotide-bound or trapped S1 isolates ATP-sensitive tryptophans (ASTs) emission from the total tryptophan signal. Neutral (acrylamide) quenching of the ASTs is sensitive to the binding or trapping of
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