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5535-55-7

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5535-55-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 5535-55-7 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 5,5,3 and 5 respectively; the second part has 2 digits, 5 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 5535-55:
(6*5)+(5*5)+(4*3)+(3*5)+(2*5)+(1*5)=97
97 % 10 = 7
So 5535-55-7 is a valid CAS Registry Number.
InChI:InChI=1/C8H7NO4S/c1-2-14(12,13)8-5-3-7(4-6-8)9(10)11/h2-6H,1H2

5535-55-7Relevant articles and documents

Diastereoselective Monofluorocyclopropanation Using Fluoromethylsulfonium Salts

Melngaile, Renate,Sperga, Arturs,Baldridge, Kim K.,Veliks, Janis

, p. 7174 - 7178 (2019/09/12)

Diarylfluoromethylsulfonium salts, alternatives to freons or advanced fluorinated building blocks, are bench stable and easy-to-use sources of direct fluoromethylene (:CHF) transfer to alkenes. These salts enabled development of a trans-selective monofluorinated Johnson-Corey-Chaykovsky reaction with vinyl sulfones or vinyl sulfonamides to access synthetically challenging monofluorocyclopropane scaffolds. The described method offers rapid access to monofluorinated cyclopropane building blocks with further functionalization opportunities to deliver more complex synthetic targets diastereoselectively.

Design, Synthesis, and Evaluation of 2-(arylsulfonyl)oxiranes as Cell-permeable Covalent Inhibitors of Protein Tyrosine Phosphatases

Dana, Dibyendu,Das, Tirtha K.,Kumar, Ish,Davalos, Anibal R.,Mark, Kevin J.,Ramai, Daryl,Chang, Emmanuel J.,Talele, Tanaji T.,Kumar, Sanjai

, p. 489 - 499 (2012/11/06)

A structure-based design approach has been applied to develop 2-(arylsulfonyl)oxiranes as potential covalent inhibitors of protein tyrosine phosphatases. A detailed kinetic analysis of inactivation by these covalent inhibitors reveals that this class of compounds inhibits a panel of protein tyrosine phosphatases in a time- and dose-dependent manner, consistent with the covalent modification of the enzyme active site. An inactivation experiment in the presence of sodium arsenate, a known competitive inhibitor of protein tyrosine phosphatase, indicated that these inhibitors were active site bound. This finding is consistent with the mass spectrometric analysis of the covalently modified protein tyrosine phosphatase enzyme. Additional experiments indicated that these compounds remained inert toward other classes of arylphosphate-hydrolyzing enzymes, and alkaline and acid phosphatases. Cell-based experiments with human A549 lung cancer cell lines indicated that 2-(phenylsulfonyl)oxirane (1) caused an increase in intracellular pTyr levels in a dose-dependent manner thereby suggesting its cell-permeable nature. Taken together, the newly identified 2-(arylsulfonyl)oxiranyl moiety could serve as a novel chemotype for the development of activity-based probes and therapeutic agents against protein tyrosine phosphatase superfamily of enzymes.

2-(4-Nitrophenyl)sulfonylethoxycarbonyl (Nsc) Group As a Base-Labile α-Amino Protection for Solid Phase Peptide Synthesis

Samukov, Vladimir V.,Sabirov, Aydar N.,Pozdnyakov, Pavel I.

, p. 7821 - 7824 (2007/10/02)

Base-labile 2-(4-nitrophenylsulfonyl)ethoxycarbonyl (Nsc) group is proposed for a temporary α-amino protection in the solid phase peptide synthesis.Nsc-Group is cleaved by organic bases in aprotic solvents under mild conditions similar to that used for Fmoc-group.Several Nα-Nsc amino acids are prepared and used in the solid phase synthesis of the fragment 307-318 of S-protein from bovine eye retina.

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