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2520-52-7

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2520-52-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 2520-52-7 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 2,5,2 and 0 respectively; the second part has 2 digits, 5 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 2520-52:
(6*2)+(5*5)+(4*2)+(3*0)+(2*5)+(1*2)=57
57 % 10 = 7
So 2520-52-7 is a valid CAS Registry Number.

2520-52-7Relevant articles and documents

Chemical and enzymatic synthesis of the alginate sugar nucleotide building block: GDP-D-mannuronic acid

Beswick, Laura,Ahmadipour, Sanaz,Dolan, Jonathan P.,Rejzek, Martin,Field, Robert A.,Miller, Gavin J.

, (2019/09/30)

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β-Glucose-1,6-Bisphosphate stabilizes pathological phophomannomutase2 mutants in vitro and represents a lead compound to develop pharmacological chaperones for the most common disorder of glycosylation, PMM2-CDG

Monticelli, Maria,Liguori, Ludovica,Allocca, Mariateresa,Andreotti, Giuseppina,Cubellis, Maria Vittoria

, (2019/10/22)

A large number of mutations causing PMM2-CDG, which is the most frequent disorder of glycosylation, destabilize phosphomannomutase2. We looked for a pharmacological chaperone to cure PMM2-CDG, starting from the structure of a natural ligand of phosphomannomutase2, α-glucose-1,6-bisphosphate. The compound, β-glucose-1,6-bisphosphate, was synthesized and characterized via 31P-NMR. β-glucose-1,6-bisphosphate binds its target enzyme in silico. The binding induces a large conformational change that was predicted by the program PELE and validated in vitro by limited proteolysis. The ability of the compound to stabilize wild type phosphomannomutase2, as well as frequently encountered pathogenic mutants, was measured using thermal shift assay. β-glucose-1,6-bisphosphate is relatively resistant to the enzyme that specifically hydrolyses natural esose-bisphosphates.

Facile enzymatic synthesis of sugar 1-phosphates as substrates for phosphorylases using anomeric kinases

Liu, Yuan,Nishimoto, Mamoru,Kitaoka, Motomitsu

, p. 1 - 4 (2015/02/19)

Three sugar 1-phosphates that are donor substrates for phosphorylases were produced at the gram scale from phosphoenolpyruvic acid and the corresponding sugars by the combined action of pyruvate kinase and the corresponding anomeric kinases in good yields. These sugar 1-phosphates were purified through two electrodialysis steps. α-d-Galactose 1-phosphate was finally isolated as crystals of dipotassium salts. α-d-Mannose 1-phosphate and 2-acetamido-2-deoxy-α-d-glucose 1-phosphate were isolated as crystals of bis(cyclohexylammonium) salts.

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