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118358-66-0

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118358-66-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 118358-66-0 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,1,8,3,5 and 8 respectively; the second part has 2 digits, 6 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 118358-66:
(8*1)+(7*1)+(6*8)+(5*3)+(4*5)+(3*8)+(2*6)+(1*6)=140
140 % 10 = 0
So 118358-66-0 is a valid CAS Registry Number.

118358-66-0Relevant articles and documents

Fluorescence-based detection of single nucleotide permutation in DNA via catalytically templated reaction

Pianowski, Zbigniew L.,Winssinger, Nicolas

, p. 3820 - 3822 (2007)

Templated reduction of low fluorescence azidocoumarin-PNA conjugate to high fluorescence aminocoumarin was achieved using a catalytic amount of DNA with single nucleotide resolution. The Royal Society of Chemistry.

In vitro synthesis of mucin-type O-glycans using saccharide primers comprising GalNAc-Ser and GalNAc-Thr residues

Ide, Yoshimi,Mizuno, Mamoru,Nagai, Kaori,Sakura, Ryuma,Sato, Toshinori,Takahashi, Yoshihisa,Yagi, Yuka,Yagi, Yuki,Yamamoto, Daiki

, (2022/01/14)

Mucin-type O-glycosylation of serine or threonine residue in proteins is known to be one of the major post-translational modifications. In this study, two novel alkyl glycosides, Nα-lauryl-O-(2-acetamido-2-deoxy-α-D-galactopyranosyl)-L-serineamide (GalNAc-Ser-C12) and Nα-lauryl-O-(2-acetamido-2-deoxy-α-D-galactopyranosyl)-L-threonineamide (GalNAc-Thr-C12) were synthesized as saccharide primers to prime mucin-type O-glycan biosynthesis in cells. Upon incubating human gastric cancer MKN45 cells with the saccharide primers, 22 glycosylated products were obtained, and their structures were analyzed using liquid chromatography-mass spectrometry and enzyme digestion. The amounts of glycosylated products were dependent on the amino acid residues in the saccharide primers. For example, in vitro synthesis of T antigen (Galβ1-3GalNAc), fucosyl-T (Fucα1-2Galβ1-3GalNAc), and sialyl-T (NeuAcα2-3Galβ1-3GalNAc) preferred a serine residue, whereas sialyl-Tn (NeuAcα2-6GalNAc) preferred a threonine residue. Furthermore, the glycosylated products derived from GalNAc-Ser/Thr-C12 and Gal-GalNAc-Ser/Thr-C12 using cell-free synthesis showed the same amino acid selectivity as those in the cell experiments. These results indicate that glycosyltransferases involved in the biosynthesis of mucin-type O-glycans distinguish amino acid residues conjugated to GalNAc. The saccharide primers developed in this study might be useful for comparing mucin-type oligosaccharides in cells and constructing oligosaccharide libraries to study cell function.

Amino acid derivative

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Paragraph 0013-0015, (2020/01/12)

The invention provides a novel amino acid derivative. The derivative is applied to modify a polypeptide drug to achieve the purposes of resisting degradation of a proteolytic enzyme and prolonging thehalf-life period of the drugs. The invention provides two methods for preparing the amino acid derivative.

COMPOSITIONS AND METHODS OF TREATING CANCER AND INFECTIONS USING BACTERIOPHAGE AND ITS MUTANTS

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Page/Page column 8, (2019/03/17)

Provided herein are vaccine composition comprising an antigen conjugated to a capsid, wherein the capsid comprises wild type or native sequence. Provided herein are also vaccine composition comprising an antigen conjugated to a capsid, wherein said capsid comprises at least one mutation, such as a non-natural mutation. Such compositions are useful in the treatment and prevention of pathogenic infections, inflammatory diseases, and neurodegenerative disease, and cancer, among others.

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