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35599-02-1 Usage

Chemical Properties

Brown Crystalline Solid


Different sources of media describe the Uses of 35599-02-1 differently. You can refer to the following data:
1. p-Nitrophenyl β-D-Mannopyranoside (cas# 35599-02-1) is a compound useful in organic synthesis.
2. 4-Nitrophenyl β-D-mannopyranoside has been used:as a substrate to analyze the action mechanism of Pyrococcus furiosus thermostable glycosidase (PFTG) and kinetic parameters by isothermal titration calorimetry (ITC)as a substrate for GH1-glucosidase (EaBgl1A) enzymeas a substrate for screening cucumber enzymes

Biochem/physiol Actions

4-Nitrophenyl β-D-mannopyranoside or p-Nitrophenyl-β-D-mannopyranoside is a substrate for determining the activity of β-D-mannopyranosidase, an enzyme required to study about glycoproteins structural details.

Check Digit Verification of cas no

The CAS Registry Mumber 35599-02-1 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,5,5,9 and 9 respectively; the second part has 2 digits, 0 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 35599-02:
141 % 10 = 1
So 35599-02-1 is a valid CAS Registry Number.



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

Version: 1.0

Creation Date: Aug 13, 2017

Revision Date: Aug 13, 2017


1.1 GHS Product identifier


1.2 Other means of identification

Product number -
Other names N-Acetyllactosamine-b-PNP,pnp LacNAc

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:35599-02-1 SDS

35599-02-1Relevant articles and documents

Garegg et al.

, p. 313 (1979)

Glycosynthase with broad substrate specificity-an efficient biocatalyst for the construction of oligosaccharide library

Wei, Jinhua,Lv, Xun,Lue, Yang,Yang, Gangzhu,Fu, Lifeng,Yang, Liu,Wang, Jianjun,Gao, Jianhui,Cheng, Shuihong,Duan, Qian,Jin, Cheng,Li, Xuebing

supporting information, p. 2414 - 2419 (2013/05/23)

A versatile glycosynthase (TnG-E338A) with strikingly broad substrate scope has been developed from Thermus nonproteolyticus β-glycosidase (TnG) by using site-directed mutagenesis. The practical utility of this biocatalyst has been demonstrated by the facile generation of a small library containing various oligosaccharides and a steroidal glycoside (total 25 compounds) in up to 100 % isolated yield. Moreover, an array of eight gluco-oligosaccharides has been readily synthesized by the enzyme in a one-pot, parallel reaction, which highlights its potential in the combinatorial construction of a carbohydrate library that will assist glycomic and glycotherapeutic research. Significantly, the enzyme provides a means by which glycosynthase technology may be extended to combinatorial chemistry.

Carbohydrate-carbohydrate interactions in water with glycophanes as model systems

Morales, Juan Carlos,Zurita, Dacil,Penades, Soledad

, p. 9212 - 9222 (2007/10/03)

The synthesis and conformational properties of glycophanes 2 and 3 (cyclodextrin-cyclophane hybrid receptors containing two maltose units linked by (4-hydroxymethyl) benzoic acid spacer) are described. The binding properties in water of these receptors with a series of 4-nitrophenyl glycosides with α- and β-configurations at the anomeric center have been studied using 1H NMR spectroscopy and molecular mechanics calculations. A comparison of these properties with those of glycophane 1 (an α,α-trehalose containing glycophane) and α-cyclodextrin (αCD) using the same glycosides shows the existence of a stabilizing contribution to the free energy of binding in the case of of glycophanes but not in the case of the αCD system. This contribution is due to carbohydrate-carbohydrate interactions between both host and guest lipophilic sugar surfaces. Glycophanes 1, 2, and 3 show similar α/β selectivity on binding the ligands, despite the great flexibility of 3 related to 1 and 2. Parallels are drawn between the thermodynamic behavior of these model systems and that proposed for sugar- protein interactions.


Baggett, Neil,Marsden, Brian J.

, p. 285 - 291 (2007/10/02)


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