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1470169-11-9

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1470169-11-9 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 1470169-11-9 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,4,7,0,1,6 and 9 respectively; the second part has 2 digits, 1 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 1470169-11:
(9*1)+(8*4)+(7*7)+(6*0)+(5*1)+(4*6)+(3*9)+(2*1)+(1*1)=149
149 % 10 = 9
So 1470169-11-9 is a valid CAS Registry Number.

1470169-11-9Downstream Products

1470169-11-9Relevant articles and documents

A general method for making peptide therapeutics resistant to serine protease degradation: Application to dipeptidyl peptidase IV substrates

Heard, Kathryn R.,Wu, Wengen,Li, Youhua,Zhao, Peng,Woznica, Iwona,Lai, Jack H.,Beinborn, Martin,Sanford, David G.,Dimare, Matthew T.,Chiluwal, Amrita K.,Peters, Diane E.,Whicher, Danielle,Sudmeier, James L.,Bachovchin, William W.

, p. 8339 - 8351 (2013/12/04)

Bioactive peptides have evolved to optimally fulfill specific biological functions, a fact which has long attracted attention for their use as therapeutic agents. While there have been some recent commercial successes fostered in part by advances in large-scale peptide synthesis, development of peptides as therapeutic agents has been significantly impeded by their inherent susceptibility to protease degradation in the bloodstream. Here we report that incorporation of specially designed amino acid analogues at the P1′ position, directly C-terminal of the enzyme cleavage site, renders peptides, including glucagon-like peptide-1 (7-36) amide (GLP-1) and six other examples, highly resistant to serine protease degradation without significant alteration of their biological activity. We demonstrate the applicability of the method to a variety of proteases, including dipeptidyl peptidase IV (DPP IV), dipeptidyl peptidase 8 (DPP8), fibroblast activation protein α (FAPα), α-lytic protease (αLP), trypsin, and chymotrypsin. In summary, the "P1′ modification" represents a simple, general, and highly adaptable method of generating enzymatically stable peptide-based therapeutics.

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