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143057

Sigma-Aldrich

Aldrithiol™-4

98%

Sinónimos:

4,4′-Dipyridyl disulfide, 4,4′-Dithiodipyridine

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About This Item

Fórmula empírica (notación de Hill):
C10H8N2S2
Número de CAS:
2645-22-9
Peso molecular:
220.31
EC Number:
220-158-6
MDL number:
MFCD00006423
UNSPSC Code:
12352100
PubChem Substance ID:
24848571
NACRES:
NA.22

assay

98%

form

solid

mp

76-78 °C (lit.)

solubility

95% ethanol: soluble 5%, clear, colorless to light yellow

storage temp.

2-8°C

SMILES string

S(Sc1ccncc1)c2ccncc2

InChI

1S/C10H8N2S2/c1-5-11-6-2-9(1)13-14-10-3-7-12-8-4-10/h1-8H

InChI key

UHBAPGWWRFVTFS-UHFFFAOYSA-N

Application

  • Aldrithiol™-4 was used as cosubstrate in a study to develop highly specific inhibitors against mannose-binding lectin-associated serine proteases by in vitro evolution technology:phage display.
  • It was used to study the O2 equilibria of recombinant human neuroglobin and cytoglobin measured under close to physiological conditions.
  • It was used to modify gold surfaces for protein studies.

Legal Information

Aldrithiol is a trademark of Sigma-Aldrich Co. LLC

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Gloves

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Leonid S Brown et al.
Journal of molecular biology, 317(3), 471-478 (2002-04-02)
The conformation of the structured EF interhelical loop of bacteriorhodopsin and its change in the M photointermediate were assessed by measuring the rate of reaction of 16 single engineered cysteine residues along the loop with water-soluble sulfhydryl reagents. The exposure
Nikitas Bistolas et al.
Biochemical and biophysical research communications, 314(3), 810-816 (2004-01-27)
The spectroelectrochemistry of camphor-bound cytochrome P450cam (P450cam) using gold electrodes is described. The electrodes were modified with either 4,4(')-dithiodipyridin or sodium dithionite. Electrolysis of P450cam was carried out when the enzyme was in solution, while at the same time UV-visible
Shwu-Jiuan Sheu et al.
Investigative ophthalmology & visual science, 44(3), 1237-1244 (2003-02-26)
To identify the mechanisms by which oxidative stress with oxidizing agents alters the activity of ion channels in human retinal pigment epithelial (RPE) cells. The effects of oxidizing agents on ion currents were investigated in human RPE R-50 cells with
Iveta Imriskova-Sosova et al.
Biochemistry, 44(51), 16949-16956 (2005-12-21)
Members of the Sco protein family are implicated in the assembly of the respiratory complex cytochrome c oxidase. Several possible roles have been proposed for Sco: a copper delivery agent, a site-specific thiol reductase, and an indicator of cellular redox
F Peter Guengerich et al.
Biochemistry, 42(37), 10965-10970 (2003-09-17)
The active site cysteine of human O(6)-alkylguanine-DNA alkyltransferase (hAGT), Cys145, was shown to be highly reactive with model electrophiles unrelated to substrates, including 1-chloro-2,4-dinitrobenzene. The high reactivity suggested that the Cys145 thiolate anion might be stable at neutral pH. The
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