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tert-butyl {4-[((2S)-2-{[N-(biphenyl-3-yl)-L-leucyl]amino}butyl)amino]phenoxy}acetate is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

757975-87-4

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757975-87-4 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 757975-87-4 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 7,5,7,9,7 and 5 respectively; the second part has 2 digits, 8 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 757975-87:
(8*7)+(7*5)+(6*7)+(5*9)+(4*7)+(3*5)+(2*8)+(1*7)=244
244 % 10 = 4
So 757975-87-4 is a valid CAS Registry Number.

757975-87-4Downstream Products

757975-87-4Relevant academic research and scientific papers

4-Aminophenoxyacetic acids as a novel class of reversible cathepsin K inhibitors

Shinozuka, Tsuyoshi,Shimada, Kousei,Matsui, Satoshi,Yamane, Takahiro,Ama, Mayumi,Fukuda, Takeshi,Taki, Motohiko,Naito, Satoru

, p. 1502 - 1505 (2007/10/03)

We have designed and synthesized a novel series of 3-biphenylamino acid amides as cathepsin K inhibitors based on compound I. In these inhibitors, we have discovered 4-aminophenoxyacetic acids 43 and 47 with good IC50 values, although lipophili

Potent and selective cathepsin K inhibitors

Shinozuka, Tsuyoshi,Shimada, Kousei,Matsui, Satoshi,Yamane, Takahiro,Ama, Mayumi,Fukuda, Takeshi,Taki, Motohiko,Takeda, Yuko,Otsuka, Eri,Yamato, Michiko,Mochizuki, Shin-ichi,Ohhata, Keiko,Naito, Satoru

, p. 6789 - 6806 (2007/10/03)

A novel series of cathepsin K inhibitors derived from Novartis compound I is described. Optimization of the P1, P3, and P1′ units led to the identification of 4-aminophenoxyacetic acid 24b with an IC50 value of 4.8 nM, which possessed an excell

Arylamine based cathepsin K inhibitors: Investigating P3 heterocyclic substituents

Shinozuka, Tsuyoshi,Shimada, Kousei,Matsui, Satoshi,Yamane, Takahiro,Ama, Mayumi,Fukuda, Takeshi,Taki, Motohiko,Takeda, Yuko,Otsuka, Eri,Yamato, Michiko,Naito, Satoru

, p. 6807 - 6819 (2007/10/03)

A modification of novel cathepsin K inhibitors I was carried out. The structural design was aimed at reducing the lipophilic character of compounds I for obtaining better pharmacokinetic profiles. This modification afforded several less lipophilic compoun

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