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436853-00-8

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436853-00-8 Usage

Description

PhenylMethyl 2-O-[2-(AcetylaMino)-2-deoxy-D-glucopyranosyl]-α-D-Mannopyranoside is a complex organic compound derived from Benzyl α-D-mannopyranoside through a specific enzymatic reaction. It is formed by α-3-D-mannoside by the enzyme UDP-GlcNAc:α-3-D-mannoside β1,2-N-acetylglucosaminyltransferase I.2 in humans. PhenylMethyl 2-O-[2-(AcetylaMino)-2-deoxy-D-glucopyranosyl]-α-D-Mannopyranoside is characterized by its unique chemical structure, which may have potential applications in various fields due to its specific functional groups and interactions.

Uses

Used in Pharmaceutical Industry:
PhenylMethyl 2-O-[2-(AcetylaMino)-2-deoxy-D-glucopyranosyl]-α-D-Mannopyranoside is used as a key intermediate in the synthesis of various pharmaceutical compounds. Its unique structure allows for the development of new drugs with potential applications in treating different diseases.
Used in Chemical Research:
PhenylMethyl 2-O-[2-(AcetylaMino)-2-deoxy-D-glucopyranosyl]-α-D-Mannopyranoside is also used as a research tool in the field of organic chemistry, particularly in the study of carbohydrate chemistry and enzyme-catalyzed reactions. Its synthesis and functionalization can provide insights into the development of new chemical methodologies and the understanding of biological processes involving carbohydrates.
Used in Drug Delivery Systems:
PhenylMethyl 2-O-[2-(AcetylaMino)-2-deoxy-D-glucopyranosyl]-α-D-Mannopyranoside can be employed in the design of drug delivery systems, taking advantage of its unique chemical structure and functional groups. It may be used to improve the targeting, bioavailability, and overall efficacy of therapeutic agents.
Used in Material Science:
PhenylMethyl 2-O-[2-(AcetylaMino)-2-deoxy-D-glucopyranosyl]-α-D-Mannopyranoside may also find applications in the field of material science, where its unique properties can be utilized in the development of new materials with specific characteristics, such as improved mechanical strength, thermal stability, or biocompatibility.

Check Digit Verification of cas no

The CAS Registry Mumber 436853-00-8 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 4,3,6,8,5 and 3 respectively; the second part has 2 digits, 0 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 436853-00:
(8*4)+(7*3)+(6*6)+(5*8)+(4*5)+(3*3)+(2*0)+(1*0)=158
158 % 10 = 8
So 436853-00-8 is a valid CAS Registry Number.

436853-00-8SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017

1.Identification

1.1 GHS Product identifier

Product name N-[(2S,3R,4R,5S,6R)-2-[(2S,3S,4S,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-2-phenylmethoxyoxan-3-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)oxan-3-yl]acetamide

1.2 Other means of identification

Product number -
Other names Phenylmethyl 2-O-[2-(Acetylamino)-2-deoxy-D-glucopyranosyl]-|A-D-mannopyranoside

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:436853-00-8 SDS

436853-00-8Downstream Products

436853-00-8Relevant articles and documents

Effects of length and amino acid sequence of O-mannosyl peptides on substrate specificity of protein O-linked mannose β1,2-N-acetylglucosaminyltransferase 1 (POMGnT1)

Akasaka-Manya, Keiko,Manya, Hiroshi,Mizuno, Mamoru,Inazu, Toshiyuki,Endo, Tamao

experimental part, p. 632 - 636 (2012/07/13)

Protein O-linked mannose β1,2- N-acetylglucosaminyltransferase 1 (POMGnT1) catalyzes the transfer of GlcNAc to O-mannose of glycoproteins. Mutations in the POMGnT1 gene cause muscle-eye-brain disease (MEB). POMGnT1 is a typical type II membrane protein, which is localized in the Golgi apparatus. However, details of the catalytic and reaction mechanism of POMGnT1 are not understood. To develop a better understanding of POMGnT1, we examined the substrate specificity of POMGnT1 using a series of synthetic O-mannosyl peptides based on the human α-dystroglycan (α-DG) sequence as substrates. O-Mannosyl peptides consisting of three to 20 amino acids are recognized as substrates. Enzyme kinetics improved with increasing peptide length up to a length of 8 amino acids but the kinetics of peptides longer than 8 amino acids were similar to those of octapeptides. Our results also show that the amino acid sequence affects POMGnT1 activity. These data suggest that both length and amino acid sequence of mannosyl peptides are determinants of POMGnT1 substrate specificity.

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