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Z-Ala-O-hexafluorisopropyl, also known as Z-protected alanine with a hexafluoroisopropyl (HFIP) group, is a chemical compound that consists of an alanine amino acid with a benzyloxycarbonyl (Z) protecting group and a hexafluoroisopropyl (HFIP) ester group attached to the hydroxyl group of the serine residue. Z-Ala-O-hexafluorisopropyl is commonly used in peptide synthesis as a building block, where the Z group protects the amino group from unwanted side reactions, and the HFIP group provides stability and solubility in organic solvents. The use of Z-Ala-O-hexafluorisopropyl allows for the controlled formation of peptide bonds and the synthesis of complex peptide sequences with minimal side reactions, making it a valuable tool in the field of biochemistry and pharmaceutical research.

71785-39-2

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71785-39-2 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 71785-39-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,1,7,8 and 5 respectively; the second part has 2 digits, 3 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 71785-39:
(7*7)+(6*1)+(5*7)+(4*8)+(3*5)+(2*3)+(1*9)=152
152 % 10 = 2
So 71785-39-2 is a valid CAS Registry Number.

71785-39-2Downstream Products

71785-39-2Relevant academic research and scientific papers

Hexafluoro-2-propanol as a potent cosolvent for chemical ligation of membrane proteins

Shen, Fei,Tang, Shan,Liu, Lei

experimental part, p. 110 - 116 (2012/01/03)

The study on membrane proteins is an important challenge mainly because of their very poor solubility in various solvents. The traditional recombinant expression strategy and the native chemical ligation method both have difficulty in generating sufficient amounts of desired proteins with high efficiency. Previous studies have shown that multiply fluorinated alcohols exhibit good ability to dissolve difficult peptide sequences, especially hexafluoro-2- propanol (HFIP). In the present study we systematically studied the capability of solvents containing different percentage of HFIP in dissolving transmembrane peptides. Through both HPLC and UV analyses we concluded that 60% HFIP/8 M urea constituted a good solvent system. In this solvent system we also optimized conditions to perform native chemical ligation (NCL). Under the optimized conditions we successfully achieved NCL's for both dipeptide formation and the synthesis of a model protein (Trifolitoxin). These results suggested that HFIP was a potential cosolvent that could be used in the ligation of poorly soluble peptides for the generation of membrane proteins.

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