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175134-34-6

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175134-34-6 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 175134-34-6 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,7,5,1,3 and 4 respectively; the second part has 2 digits, 3 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 175134-34:
(8*1)+(7*7)+(6*5)+(5*1)+(4*3)+(3*4)+(2*3)+(1*4)=126
126 % 10 = 6
So 175134-34-6 is a valid CAS Registry Number.

175134-34-6Downstream Products

175134-34-6Relevant articles and documents

The Synthesis of Chiral α-Aryl α-Hydroxy Carboxylic Acids via RuPHOX-Ru Catalyzed Asymmetric Hydrogenation

Guo, Huan,Li, Jing,Liu, Delong,Zhang, Wanbin

, p. 3665 - 3673 (2017/09/11)

A ruthenocenyl phosphino-oxazoline-ruthenium complex (RuPHOX?Ru) catalyzed asymmetric hydrogenation of α-aryl keto acids has been successfully developed, affording the corresponding chiral α-aryl α-hydroxy carboxylic acids in high yields and with up to 97% ee. The reaction could be performed on a gram scale with a relatively low catalyst loading (up to 5000 S/C) and the resulting products can be transformed to several chiral building blocks, biologically active compounds and chiral drugs. (Figure presented.).

Production Of Enantiopure alpha-Hydroxy Carboxylic Acids From Alkenes By Cascade Biocatalysis

-

Paragraph 0089; 0090, (2016/05/02)

The invention provides compositions comprising an alkene epoxidase and a selective epoxide hydrolase, such as a recombinant microorganism comprising a first heterologous nucleic acid encoding an alkene epoxidase and a second heterologous nucleic acid encoding a selective epoxide hydrolase. Exemplary alkene epoxidases include StyAB, while exemplary selective epoxide hydrolases include epoxide hydrolases from Sphingomonas, Solanum tuberosum, or Aspergillus. The invention also provides non-toxic methods of making enantiomerically pure vicinal diols or enantiomerically pure alpha-hydroxy carboxylic acids using these compositions and microorganisms.

Robust enzymatic resolution of 3-fluoromandelic acid with lipase PS supported on celite

Mendiola, Javier,Garcia-Cerrada, Susana,De Frutos, Oscar,De La Puente, Maria Luz

experimental part, p. 1312 - 1316 (2012/10/18)

The resolution of different mandelic acids using the lipase PS Amano SD enzyme is described. By supporting the lyophilized enzyme over Celite, both the activity and the stability of lipase PS in organic media were significantly improved, enabling the robust resolution scale-up of 3-fluoromandelic acid. The methodology was extended to produce a range of optically pure (R)-mandelic acids, avoiding tedious extractions or chromatography.

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