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1169765-66-5

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1169765-66-5 Usage

General Description

Cbz-3-Chloro-D-Phenylalanine is a chemical compound that belongs to the family of amino acids and derivatives. It is a modified form of the amino acid phenylalanine, in which a chlorine atom is added to the third carbon position and protected with a carbobenzyloxy group. Cbz-3-Chloro-D-Phenylalanine has a wide range of potential applications, including as a building block in the synthesis of pharmaceuticals and as a tool for studying the structure and function of proteins. It may also have potential therapeutic applications due to its ability to interact with biological targets in the body. The compound is typically synthesized in the laboratory using various chemical reactions and purification techniques to produce a high-purity product for research and commercial use.

Check Digit Verification of cas no

The CAS Registry Mumber 1169765-66-5 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,1,6,9,7,6 and 5 respectively; the second part has 2 digits, 6 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 1169765-66:
(9*1)+(8*1)+(7*6)+(6*9)+(5*7)+(4*6)+(3*5)+(2*6)+(1*6)=205
205 % 10 = 5
So 1169765-66-5 is a valid CAS Registry Number.

1169765-66-5Relevant articles and documents

Discovery of Fluoromethylketone-Based Peptidomimetics as Covalent ATG4B (Autophagin-1) Inhibitors

Qiu, Zongxing,Kuhn, Bernd,Aebi, Johannes,Lin, Xianfeng,Ding, Haiyuan,Zhou, Zheng,Xu, Zhiheng,Xu, Danqing,Han, Li,Liu, Cheng,Qiu, Hongxia,Zhang, Yuxia,Haap, Wolfgang,Riemer, Claus,Stahl, Martin,Qin, Ning,Shen, Hong C.,Tang, Guozhi

supporting information, p. 802 - 806 (2016/08/24)

ATG4B or autophagin-1 is a cysteine protease that cleaves ATG8 family proteins. ATG4B plays essential roles in the autophagosome formation and the autophagy pathway. Herein we disclose the design and structural modifications of a series of fluoromethylketone (FMK)-based peptidomimetics as highly potent ATG4B inhibitors. Their structure-activity relationship (SAR) and protease selectivity are also discussed.

α-chymotrypsin-catalysed peptide synthesis via the kinetically controlled approach using activated esters as acyl donors in organic solvents with low water content: Incorporation of non-protein amino acids into peptides

Miyazawa, Toshifumi,Nakajo, Shin'ichi,Nishikawa, Miyako,Hamahara, Kazumi,Imagawa, Kiwamu,Ensatsu, Eiichi,Yanagihara, Ryoji,Yamada, Takashi

, p. 82 - 86 (2007/10/03)

The α-chymotrypsin-catalyzed peptide synthesis via the kinetically controlled approach using activated esters as acyl donors in orgnanic solvents with low water content was presented. The methyl esters of N-Z derivatives of racemic non-protein amino acids were chosen as carboxy components. They allowed the peptide-bond formation and optical resolution simultaneously to yield homochiral peptides. This method is useful for the incorporation of non-protein amino acids into peptides.

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