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About This Item
Empirical Formula (Hill Notation):
C29H42N2O3S
CAS Number:
Molecular Weight:
498.72
UNSPSC Code:
12171500
PubChem Substance ID:
MDL number:
InChI
1S/C29H42N2O3S/c1-3-5-9-22-31(23-10-6-4-2)29-17-15-27(16-18-29)13-7-8-14-28-19-24-30(25-20-28)21-11-12-26-35(32,33)34/h7-8,13-20,24-25H,3-6,9-12,21-23,26H2,1-2H3
SMILES string
CCCCCN(CCCCC)c1ccc(\C=C\C=C/c2cc[n+](CCCCS([O-])(=O)=O)cc2)cc1
InChI key
URNCTMHGJQSLOC-UHFFFAOYSA-N
assay
≥95%
form
solid
color
red
solubility
DMF: soluble, DMSO: soluble, ethanol: soluble
storage temp.
2-8°C
Biochem/physiol Actions
Chromogenic substrate for β-galactosidase that generates red or magenta precipitate on hydrolysis.
Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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V L Shapovalov et al.
Biophysical journal, 77(1), 299-305 (1999-07-02)
The effect of channel-forming peptide gramicidin A on the dipole potential of phospholipid monolayers and bilayers has been studied. Surface pressure and surface potential isotherms of monolayers have been measured with a Langmuir trough equipped with a Wilhelmy balance and
A Schneeberger et al.
The Journal of membrane biology, 168(3), 221-228 (1999-04-07)
To investigate Na+ binding to the ion-binding sites presented on the cytoplasmic side of the Na,K-ATPase, equilibrium Na+-titration experiments were performed using two fluorescent dyes, RH421 and FITC, to detect protein-specific actions. Fluorescence changes upon addition of Na+ in the
F Cornelius
Biophysical journal, 77(2), 934-942 (1999-07-29)
Phosphorylation of shark rectal Na,K-ATPase by ATP in the presence of Na(+) was characterized by chemical quench experiments and by stopped-flow RH421 fluorescence. The appearance of acid-stable phosphoenzyme was faster than the rate of fluorescence increase, suggesting that of the
A Grinvald et al.
Biophysical journal, 42(2), 195-198 (1983-05-01)
To improve the sensitivity of fluorescence measurements of electrical responses from small cells and their processes, we have optimized the optical measuring system. The fluorescence intensity from a stained cell was increased 40-fold relative to our previous apparatus. The increased
Anne Pilotelle-Bunner et al.
Biophysical journal, 96(9), 3753-3761 (2009-05-06)
The Mg(2+) dependence of the kinetics of the phosphorylation and conformational changes of Na(+),K(+)-ATPase was investigated via the stopped-flow technique using the fluorescent label RH421. The enzyme was preequilibrated in buffer containing 130 mM NaCl to stabilize the E1(Na(+))(3) state.
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