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<(1R)-1-amino>-3-methylbutyl>phosphonic acid is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

128948-77-6

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128948-77-6 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 128948-77-6 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,2,8,9,4 and 8 respectively; the second part has 2 digits, 7 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 128948-77:
(8*1)+(7*2)+(6*8)+(5*9)+(4*4)+(3*8)+(2*7)+(1*7)=176
176 % 10 = 6
So 128948-77-6 is a valid CAS Registry Number.

128948-77-6Relevant academic research and scientific papers

A mild and convenient oxidation of H-phosphinic acids

Berlicki,Mucha,Kafarski

, p. 1959 - 1962 (2008/09/19)

A new mild and convenient method of oxidation of H-phosphinic to the corresponding phosphonic acids was developed. Conversion of H-phosphinic acids into trivalent trimethylsilyl esters using hexamethyldisilazane, followed by their oxidation with air and subsequent methanolysis allowed obtaining the final compounds in good to excellent yields. The methodology was proved to be particularly useful for N-benzyloxycarbonyl-α-aminophosphinic acids. The scope and limitations of the reaction were additionally tested using a variety of both free and protected amino- and hydroxyphosphinates as substrates.

Thiourea-Catalyzed Enantioselective Hydrophosphonylation of Imines: Practical Access to Enantiomerically Enriched α-Amino Phosphonic Acids

Joly, Guy D.,Jacobsen, Eric N.

, p. 4102 - 4103 (2007/10/03)

Chiral thiourea 1b catalyzes the highly enantioselective hydrophosphonylation of a wide range of N-benzyl imines. The hydrophosphonylation products are readily deprotected by hydrogenolysis, providing access to free α-amino phosphonic acids in highly enantioenriched form. Copyright

Potent Inhibition of Pepsin and Penicillopepsin by Phosphorus-Containing Peptide Analogues

Bartlett, Paul A.,Hanson, John E.,Giannousis, Peter P.

, p. 6268 - 6274 (2007/10/02)

Phosphinic and phosphonic acid peptide derivatives have been evaluated as inhibitors of the aspartic proteases pepsin and penicillopepsin.The most potent of those studied is isovaleryl-Val-Val-LeuP-(O)Phe-Ala-Ala-OMe (4) (LeuP repres

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