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39225

Sigma-Aldrich

5-(Dimethylamino)-1-naphthalenesulfonamide

for fluorescence, ≥98.5% (TLC)

Synonym(s):

DNSA, Dansyl amide

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About This Item

Linear Formula:
(CH3)2NC10H6SO2NH2
CAS Number:
1431-39-6
Molecular Weight:
250.32
Beilstein:
2217203
EC Number:
215-854-1
MDL number:
MFCD00004000
UNSPSC Code:
12352100
PubChem Substance ID:
329755829

grade

for fluorescence

Assay

≥98.5% (TLC)

form

solid

mp

218-221 °C (lit.)

SMILES string

CN(C)c1cccc2c(cccc12)S(N)(=O)=O

InChI

1S/C12H14N2O2S/c1-14(2)11-7-3-6-10-9(11)5-4-8-12(10)17(13,15)16/h3-8H,1-2H3,(H2,13,15,16)

InChI key

TYNBFJJKZPTRKS-UHFFFAOYSA-N

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Other Notes

Active-site probe for carbonic anhydrase

replaced by

Product No.
Description
Pricing

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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R W Henkens et al.
Biochemistry, 21(23), 5918-5923 (1982-11-09)
Particularly stable elements of noncovalent structure in bovine carbonic anhydrase have been detected and studied. These are present in a highly populated intermediate state formed during denaturation of the enzyme with guanidinium chloride. The intermediate has been detected by analysis
Harmen P Dijkstra et al.
Organic & biomolecular chemistry, 6(3), 523-531 (2008-01-26)
Reactive phosphonates are important probes to target the active site of serine hydrolases, one of the largest and most diverse family of enzymes. Developing such inhibitory probes is of special importance in activity based protein profiling, a strategy that is
P Billsten et al.
FEBS letters, 402(1), 67-72 (1997-01-27)
Human carbonic anhydrase II pseudo-wild type (HCAIIpwt) and two truncated variants were adsorbed to approximately 9 nm silica nanoparticles. Ellipsometry was used as an indirect measure of protein adsorption. The structural changes of adsorbed proteins were investigated with the use
Ereny F Morcos et al.
Electrophoresis, 31(22), 3691-3695 (2010-10-26)
Back-scattering interferometry (BSI) is a label-free, free-solution, small-volume technique used for characterizing binding interactions, which is also relevant to a growing number of biosensing applications including drug discovery. Here, we use BSI to characterize the interaction of carbonic anhydrase enzyme
Abir L Banerjee et al.
Biochemistry, 44(9), 3211-3224 (2005-03-02)
Benzenesulfonamide and iminodiacetate (IDA)-conjugated Cu(2+) independently interact at the active site and a peripheral site of carbonic anhydrases, respectively [Banerjee, A. L., Swanson, M., Roy, B. C., Jia, X., Haldar, M. K., Mallik, S., and Srivastava, D. K. (2004) J.
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