Grade
for fluorescence
분석
≥99.0% (HPLC)
mp
218-220 °C (lit.)
형광
λex 398 nm; λem 482 nm in 0.1 M phosphate pH 7.0 (after derivatization with 2-mercaptoethanol)
적합성
suitable for fluorescence
SMILES string
CN(C)c1ccc2C(C)=C(N3C(=O)C=CC3=O)C(=O)Oc2c1
InChI
1S/C16H14N2O4/c1-9-11-5-4-10(17(2)3)8-12(11)22-16(21)15(9)18-13(19)6-7-14(18)20/h4-8H,1-3H3
InChI key
ADEORFBTPGKHRP-UHFFFAOYSA-N
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기타 정보
Fluorescent reagent with high selectivity for protein thiols and with superior fluorescence and water solubility properties than dansyl chloride
가장 최신 버전 중 하나를 선택하세요:
Y. Kanaoka
Angewandte Chemie (International Edition in English), 89, 141-141 (1977)
T Ohyashiki et al.
Journal of biochemistry, 115(2), 224-229 (1994-02-01)
The effects of lipid peroxidation on the SH reactivity of the proteins in porcine intestinal brush-border membranes were examined using a fluorogenic thiol reagent, N-[7-dimethyl-amino-4-methylcoumarinyl]maleimide (DACM) in relation to lipid organization. Changes in the lipid organization were assessed by measurement
L A Jurado et al.
Biochimica et biophysica acta, 1292(1), 188-196 (1996-01-04)
We studied the transition metal ion requirements for activity and sulfhydryl group reactivity in phospho enol pyruvate carboxykinase (PEP-carboxykinase; ATP:oxaloacetate carboxylase (transphosphorylating), EC 4.1.1.49), a key enzyme in the energy metabolism of the protozan parasite Trypanosoma (Schizotrypanum) cruzi. As for
Kuikui Wang et al.
Talanta, 84(2), 400-405 (2011-03-08)
A sensitive and selective method for the paraoxon detection based on enzyme inhibition and fluorescence quenching was presented in this study. Under the catalytic effect of acetylcholinesterase (AChE), acetylthiocholine (ATCh) hydrolysis released thiocholine (TCh) which could react with N-(7-dimethylamino-4-methylcoumarin-3-yl) maleimide
M Hatanaka et al.
Biochimica et biophysica acta, 1209(1), 117-122 (1994-11-16)
Purified C9 with expected hemolytic and polymerizing activities was found to contain approximately 0.2 mol of sulfhydryl groups/mol of C9. By proteolysis of C9 with labeled SH groups, the SH residues on intact C9 were mapped to Cys-359 and Cys-384
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