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86925-99-7

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86925-99-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 86925-99-7 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 8,6,9,2 and 5 respectively; the second part has 2 digits, 9 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 86925-99:
(7*8)+(6*6)+(5*9)+(4*2)+(3*5)+(2*9)+(1*9)=187
187 % 10 = 7
So 86925-99-7 is a valid CAS Registry Number.

86925-99-7SDS

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 benzyl (2S)-2-(naphthalen-2-ylcarbamoyl)pyrrolidine-1-carboxylate

1.2 Other means of identification

Product number -
Other names (S)-1-benzyloxycarbonyl-N-(2-naphthyl)-2-pyrrolidinecarboxamide

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:86925-99-7 SDS

86925-99-7Relevant articles and documents

POST-PROLINE ENDOPEPTIDASE. PARTIAL PURIFICATION AND CHARACTERIZATION OF THE ENZYME FROM PIG KIDNEYS

Hauzer, Karel,Servitova, Linda,Barth, Tomislav,Jost, Karel

, p. 1139 - 1148 (2007/10/02)

Post-proline endopeptidase was isolated from pig kidneys and partially purified.The procedure consisted of fractionation with ammonium sulphate, ion exchange chromatography on DEAE-Sephadex A-50, gel filtration on Sephadex G-200 and rechromatography on DEAE-Sephadex A-50.The preparation had 55 times higher specific activity than the crude extract and did not contain any contaminating enzymic activities.The enzyme cleaved a number of proline-containing peptides and was strictly specific in catalyzing the hydrolysis of the peptide bond on the carboxyl side of the proline residue.The optimum pH for the hydrolysis of the synthetic peptides benzyloxycarbonylglycyl-prolyl-leucyl-glycinamide and benzyloxycarbonyl-glycyl-proline β-naphthylamide was 7.8-8.0 and, in the case of benzyloxycarbonylglycyl-proline p-nitroanilide, 7.2 to 7.5.For the hydrolysis of the tetrapeptide benzyloxycarbonylglycyl-prolyl-leucyl-glycinamide, the Km value of 75 μmol l-1 was obtained.

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