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70497-50-6

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  • benzyl N-[1-[(1-carbamoyl-2-methyl-propyl)carbamoyl]ethyl]carbamate

    Cas No: 70497-50-6

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70497-50-6 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 70497-50-6 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,0,4,9 and 7 respectively; the second part has 2 digits, 5 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 70497-50:
(7*7)+(6*0)+(5*4)+(4*9)+(3*7)+(2*5)+(1*0)=136
136 % 10 = 6
So 70497-50-6 is a valid CAS Registry Number.

70497-50-6SDS

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 benzyl N-[1-[(1-amino-3-methyl-1-oxobutan-2-yl)amino]-1-oxopropan-2-yl]carbamate

1.2 Other means of identification

Product number -
Other names -

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:70497-50-6 SDS

70497-50-6Downstream Products

70497-50-6Relevant articles and documents

Mechanoenzymatic peptide and amide bond formation

Hernández, José G.,Ardila-Fierro, Karen J.,Crawford, Deborah,James, Stuart L.,Bolm, Carsten

supporting information, p. 2620 - 2625 (2017/07/17)

Mechanochemical chemoenzymatic peptide and amide bond formation catalysed by papain was studied by ball milling. Despite the high-energy mixing experienced inside the ball mill, the biocatalyst proved stable and highly efficient to catalyse the formation of α,α- and α,β-dipeptides. This strategy was further extended to the enzymatic acylation of amines by milling, and to the mechanosynthesis of a derivative of the valuable dipeptide L-alanyl-l-glutamine.

Pronase catalysed peptide syntheses

Lobell, Mario,Schneider, Manfred P.

, p. 319 - 325 (2007/10/03)

A mixture of proteases from Streptomyces griseus (pronase), displaying a very broad substrate tolerance in the hydrolysis of peptides, has been studied for the first time systematically regarding their substrate specificity in peptide synthesis. It is demonstrated that pronase can be employed successfully for the formation of dipeptides with yields up to 95%. Pronase has also been employed successfully as catalyst for the enzyme assisted synthesis of a hexapeptide.

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