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4257-96-9

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4257-96-9 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 4257-96-9 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 4,2,5 and 7 respectively; the second part has 2 digits, 9 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 4257-96:
(6*4)+(5*2)+(4*5)+(3*7)+(2*9)+(1*6)=99
99 % 10 = 9
So 4257-96-9 is a valid CAS Registry Number.

4257-96-9Downstream Products

4257-96-9Relevant articles and documents

PROCESS OF SYNTHESIS OF β-6'SULFOQUINOVOSYL DIACYLGLYCEROLS

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Page/Page column 11; 12, (2022/02/28)

The present invention relates to a synthesis process of β-6-sulfoquinovosyl-diacylglycerols. In particular, said process is for the synthesis of the compounds 1,2-O-distearoyl-3-O-(β- sulfoquinovosyl)-R/S-glycerol, 1,2-O-distearoyl-3-O-(β-sulfoquinovosyl)-R-glycerol or 1,2- O-distearoyl-3-O-(β-sulfoquinovosyl)-S-glycerol, named respectively Sulfavant A, Sulfavant R and Sulfavant S.

Selectivity of 1-O-Propargyl-D-Mannose Preparations

?ezanka, Michal,Dolensky, Bohumil,Krabicová, Ilona

, (2022/03/01)

Thanks to their ability to bind to specific biological receptors, mannosylated structures are examined in biomedical applications. One of the most common ways of linking a functional moiety to a structure is to use an azide-alkyne click reaction. Therefore, it is necessary to prepare and isolate a propargylated mannose derivative of high purity to maintain its bioactivity. Three known preparations of propargyl-α-mannopyranoside were revisited, and products were analysed by NMR spectroscopy. The preparations were shown to yield by-products that have not been described in the literature yet. Our experiments showed that one-step procedures could not provide pure propargyl-α-mannopyranoside, while a three-step procedure yielded the desired compound of high purity.

A Sweet H2S/H2O2Dual Release System and Specific Protein S-Persulfidation Mediated by Thioglucose/Glucose Oxidase

Ni, Xiang,Li, Xiaolu,Shen, Tun-Li,Qian, Wei-Jun,Xian, Ming

supporting information, p. 13325 - 13332 (2021/09/03)

H2S and H2O2 are two redox regulating molecules that play important roles in many physiological and pathological processes. While each of them has distinct biosynthetic pathways and signaling mechanisms, the crosstalk between these two species is also known to cause critical biological responses such as protein S-persulfidation. So far, many chemical tools for the studies of H2S and H2O2 have been developed, such as the donors and sensors for H2S and H2O2. However, these tools are normally targeting single species (e.g., only H2S or only H2O2). As such, the crosstalk and synergetic effects between H2S and H2O2 have hardly been studied with those tools. In this work, we report a unique H2S/H2O2 dual donor system by employing 1-thio-β-d-glucose and glucose oxidase (GOx) as the substrates. This enzymatic system can simultaneously produce H2S and H2O2 in a slow and controllable fashion, without generating any bio-unfriendly byproducts. This system was demonstrated to cause efficient S-persulfidation on proteins. In addition, we expanded the system to thiolactose and thioglucose-disulfide; therefore, additional factors (β-galactosidase and cellular reductants) could be introduced to further control the release of H2S/H2O2. This dual release system should be useful for future research on H2S and H2O2.

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