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120221-14-9

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  • Featured products (2S,3R,4S,5S,6R)-2-(2-chloro-4-nitrophenoxy)-6-(hydroxymethyl)oxane-3,4,5-triol

    Cas No: 120221-14-9

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  • Factory Price API 99% 2-Chloro-4-(nitrophenyl)-B-D-glucopyranoside CAS 120221-14-9 GMP Manufacturer

    Cas No: 120221-14-9

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120221-14-9 Usage

General Description

2-CHLORO-4-NITROPHENYL-BETA-D-GLUCO-PYRANOSIDE is a chemical compound used in biochemical research as a substrate for beta-glucosidase enzymes. It contains a glucose moiety attached to a phenyl ring substituted with a chloro and nitro group. 2-CHLORO-4-NITROPHENYL-BETA-D-GLUCO- PYRANOSIDE* is commonly used in enzymatic assays to study the activity and specificity of beta-glucosidase enzymes, which play a role in carbohydrate metabolism and the breakdown of glycosidic bonds. The presence of the chloro and nitro groups make this compound useful for monitoring enzyme kinetics and assessing potential inhibitors of beta-glucosidase activity.

Check Digit Verification of cas no

The CAS Registry Mumber 120221-14-9 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,2,0,2,2 and 1 respectively; the second part has 2 digits, 1 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 120221-14:
(8*1)+(7*2)+(6*0)+(5*2)+(4*2)+(3*1)+(2*1)+(1*4)=49
49 % 10 = 9
So 120221-14-9 is a valid CAS Registry Number.

120221-14-9SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 16, 2017

Revision Date: Aug 16, 2017

1.Identification

1.1 GHS Product identifier

Product name (2S,3R,4S,5S,6R)-2-(2-chloro-4-nitrophenoxy)-6-(hydroxymethyl)oxane-3,4,5-triol

1.2 Other means of identification

Product number -
Other names (2S,3R,4S,5S,6R)-2-(2-Chloro-4-nitrophenoxy)-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol

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:120221-14-9 SDS

120221-14-9Relevant articles and documents

An Efficient Strategy for the Chemo-Enzymatic Synthesis of Bufalin Glycosides with Improved Water Solubility and Inhibition against Na+, K+-ATPase

Liu, Yan,Xu, Wei,Huang, Zhao-He,Guo, Jun,Jiang, Ren-Wang

, (2020/10/26)

In this study, bufalin was glycosylated by an efficient chemo-enzymatic strategy. Firstly, 2-chloro-4-nitrophenyl-1-O-β-D-glucoside (sugar donors) was obtained by chemical synthesis. Then, the glycosylation of the bufalin was achieved with the synthesized sugar donor under the catalysis of two glycosyltransferases (Loki and ASP). Finally, two glycosides, i. e., bufalin-3-O-β-D-glucopyranoside and bufalin-3-O-[β-D-glucopyranosyl-(1→2)-β-D-glucopyranoside)], were obtained by preparative HPLC. Compared to our previously reported sole chemical (total yield 10 % in four steps) or enzymatic methods (30 %), our combined chemo-enzymatic strategy in this article greatly improves the yields of monoglycoside (68 %) and diglycoside (21 %) and decreased the experimental cost (90 %). Furthermore, we tested the water solubility of these glycosides and found that the water solubilities of the two glycosides were 13.1 and 53.7 times of bufalin, respectively. In addition, the inhibitory activity of these glycosides against Na+, K+-ATPase were evaluated. The mono-glycosylated compound showed more potent activity than bufalin, while the diglycosylated compound was less potent.

Facile and Versatile Chemoenzymatic Synthesis of Enterobactin Analogues and Applications in Bacterial Detection

Lee, Albert A.,Chen, Yi -Chen S.,Ekalestari, Elisa,Ho, Sheng -Yang,Hsu, Nai -Shu,Kuo, Tang -Feng,Wang, Tsung -Shing Andrew

supporting information, p. 12338 - 12342 (2016/10/13)

Siderophores, such as enterobactin (Ent), are small molecules that can be selectively imported into bacteria along with iron by cognate transporters. Siderophore conjugates are thus a promising strategy for delivering functional reagents into bacteria. In this work, we present an easy-to-perform, one-pot chemoenzymatic synthesis of functionalized monoglucosylated enterobactin (MGE). When functionalized MGE is conjugated to a rhodamine fluorophore, which affords RhB-Glc-Ent, it can selectively label Gram-negative bacteria that utilize Ent, including some E. coli strains and P. aeruginosa. V. cholerae, a bacterium that utilizes linearized Ent, can also be weakly targeted. Moreover, the targeting is effective under iron-limiting but not iron-rich conditions. Our results suggest that the RhB-Glc-Ent probe is sensitive not only to the bacterial strain but also to the iron condition in the environment.

Examination of the active sites of human salivary α-amylase (HSA)

Kandra, Lili,Gyemant, Gyoengyi

, p. 579 - 585 (2007/10/03)

The action pattern of human salivary amylase (HSA) was examined by utilising as model substrates 2-chloro-4-nitrophenyl (CNP) β-glycosides of maltooligosaccharides of dp 4-8 and some 4-nitrophenyl (NP) derivatives modified at the nonreducing end with a 4,6-O-benzylidene (Bnl) group. The product pattern and cleavage frequency were investigated by product analysis using HPLC. The results revealed that the binding region in HSA is longer than five subsites usually considered in the literature and suggested the presence of at least six subsites; four glycone binding sites (-4, -3, -2, -1) and two aglycone binding sites (+1, +2). In the ideal arrangement, the six subsites are filled by a glucosyl unit and the release of maltotetraose (G4) from the nonreducing end is dominant. The benzylidene group was also recognisable by subsites (-3) and (-4). The binding modes of the benzylidene derivatives indicated a favourable interaction between the Bnl group and subsite (-3) and an unfavourable one with subsite (-4). Thus, subsite (-4) must be more hydrophylic than hydrophobic. As compared with the action of porcine pancreatic α-amylase (PPA) on the same substrates, the results showed differences in the three-dimensional structure of active sites of HSA and PPA. (C) 2000 Elsevier Science Ltd.

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