39225
5-(Dimethylamino)-1-naphthalenesulfonamide
for fluorescence, ≥98.5% (TLC)
Synonym(s):
DNSA, Dansyl amide
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About This Item
Recommended Products
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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Journal of Protein Chemistry, 3, 357-357 (1984)
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
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
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
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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