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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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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
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
A Schneeberger et al.
The Journal of membrane biology, 179(3), 263-273 (2001-03-14)
In the E1 state of the Na,K-ATPase all cations present in the cytoplasm compete for the ion binding sites. The mutual effects of mono-, di- and trivalent cations were investigated by experiments with the electrochromic fluorescent dye RH421. Three sites
Nadine Harmel et al.
The Journal of general physiology, 128(1), 103-118 (2006-06-28)
The interaction of palytoxin with the Na,K-ATPase was studied by the electrochromic styryl dye RH421, which monitors the amount of ions in the membrane domain of the pump. The toxin affected the pump function in the state P-E2, independently of
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