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21685-41-6

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21685-41-6 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 21685-41-6 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,1,6,8 and 5 respectively; the second part has 2 digits, 4 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 21685-41:
(7*2)+(6*1)+(5*6)+(4*8)+(3*5)+(2*4)+(1*1)=106
106 % 10 = 6
So 21685-41-6 is a valid CAS Registry Number.

21685-41-6SDS

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 N-benzyloxycarbonyl-L-phenylalanylglycine methyl ester

1.2 Other means of identification

Product number -
Other names Cbz-Phe-Gly-OCH3

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:21685-41-6 SDS

21685-41-6Relevant articles and documents

Peptide-Chain Elongation Using Unprotected Amino Acids in a Micro-Flow Reactor

Fuse, Shinichiro,Masuda, Koshiro,Otake, Yuma,Nakamura, Hiroyuki

supporting information, p. 15091 - 15097 (2019/11/13)

Conventional peptide synthesis requires a deprotection step after each amidation step, which decreases synthetic efficiency. Therefore, peptide synthesis using unprotected amino acids is considered an ideal approach. Here, we report peptide chain elongati

Scandium(III) triflate-promoted serine/threonine-selective peptide bond cleavage

Ni, Jizhi,Sohma, Youhei,Kanai, Motomu

supporting information, p. 3311 - 3314 (2017/03/22)

The site-selective cleavage of peptide bonds is an important chemical modification that is useful not only for the structural determination of peptides, but also as an artificial modulator of peptide/protein function and properties. Here we report site-selective hydrolysis of peptide bonds at the Ser and Thr positions with a high conversion yield. This chemical cleavage relies on Sc(iii)-promoted N,O-acyl rearrangement and subsequent hydrolysis. The method is applicable to a broad scope of polypeptides with various functional groups, including a post-translationally modified peptide that is unsuitable for enzymatic hydrolysis. The system was further extended to site-selective cleavage of a native protein, Aβ1-42, which is closely related to the onset of Alzheimer's disease.

Recyclable hypervalent iodine(III) reagent iodosodilactone as an efficient coupling reagent for direct esterification, amidation, and peptide coupling

Tian, Jun,Gao, Wen-Chao,Zhou, Dong-Mei,Zhang, Chi

supporting information; experimental part, p. 3020 - 3023 (2012/08/07)

A hypervalent iodine(III) reagent plays a novel role as an efficient coupling reagent to promote the direct condensation between carboxylic acids and alcohols or amines to provide esters, macrocyclic lactones, amides, as well as peptides without racemization. The regeneration of iodosodilactone (1) can also be readily achieved. The intermediate acyloxyphosphonium ion C from the activation of a carboxylic acid is thought to be involved in the present esterification reaction.

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