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Benzeneseleninic acid, 4-nitro- is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

33350-70-8

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33350-70-8 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 33350-70-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,3,3,5 and 0 respectively; the second part has 2 digits, 7 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 33350-70:
(7*3)+(6*3)+(5*3)+(4*5)+(3*0)+(2*7)+(1*0)=88
88 % 10 = 8
So 33350-70-8 is a valid CAS Registry Number.

33350-70-8SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017

1.Identification

1.1 GHS Product identifier

Product name 4-nitro-benzeneseleninic acid

1.2 Other means of identification

Product number -
Other names p-Nitrobenzol-selenige Saeure

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:33350-70-8 SDS

33350-70-8Downstream Products

33350-70-8Relevant academic research and scientific papers

Modelling the Inhibition of Selenoproteins by Small Molecules Using Cysteine and Selenocysteine Derivatives

Reddy, Kishorkumar M.,Mugesh, Govindasamy

, p. 8875 - 8883 (2019/06/17)

Small molecule-based electrophilic compounds such as 1-chloro-2,4-dinitrobenzene (CDNB) and 1-chloro-4-nitrobenzene (CNB) are currently being used as inhibitors of cysteine- and selenocysteine-containing proteins. CDNB has been used extensively to determine the activity of glutathione S-transferase and to deplete glutathione (GSH) in mammalian cells. Also, CDNB has been shown to irreversibly inhibit thioredoxin reductase (TrxR), a selenoenzyme that catalyses the reduction of thioredoxin (Trx). Mammalian TrxR has a C-terminal active site motif, Gly-Cys-Sec-Gly, and both the cysteine and selenocysteine residues could be the targets of the electrophilic reagents. In this paper we report on the stability of a series of cysteine and selenocysteine derivatives that can be considered as models for the selenoenzyme–inhibitor complexes. We show that these derivatives react with H2O2 to generate the corresponding selenoxides, which undergo spontaneous elimination to produce dehydroalanine. In contrast, the cysteine derivatives are stable towards such elimination reactions. We also demonstrate, for the first time, that the arylselenium species eliminated from the selenocysteine derivatives exhibit significant redox activity by catalysing the reduction of H2O2 in the presence of GSH (GPx (glutathione peroxidase)-like activity), which suggests that such redox modulatory activity of selenium compounds may have a significant effect on the cellular redox state during the inhibition of selenoproteins.

Oxidation of Organic Diselenides with Hydrogen Peroxide to Alkane- and Areneseleninic Acids and Selenium-Containing Heterocycles

Kloc, Krystian,Mlochowski, Jacek,Syper, Ludwik

, p. 811 - 814 (2007/10/02)

A convenient way is reported for the oxidation of organic diselenides 1,3 to organoseleninic acids 2,4 which were isolated and identified as pure compounds.Some ortho-substituted phenyl diselenides 3d-f underwent oxidative cyclization, and the selenium-co

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