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4753-07-5

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4753-07-5 Usage

Chemical Properties

White Solid

Uses

Bromo Heptaacetyl-D-lactoside, Stabilized with 4% Calcium Carbonate (cas# 4753-07-5) is a compound useful in organic synthesis.

Check Digit Verification of cas no

The CAS Registry Mumber 4753-07-5 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 4,7,5 and 3 respectively; the second part has 2 digits, 0 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 4753-07:
(6*4)+(5*7)+(4*5)+(3*3)+(2*0)+(1*7)=95
95 % 10 = 5
So 4753-07-5 is a valid CAS Registry Number.

4753-07-5SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 19, 2017

Revision Date: Aug 19, 2017

1.Identification

1.1 GHS Product identifier

Product name Bromo Heptaacetyl-D-lactoside

1.2 Other means of identification

Product number -
Other names [(2R,3S,4S,5R,6S)-3,4,5-triacetyloxy-6-[(2R,3R,4S,5R,6R)-4,5-diacetyloxy-2-(acetyloxymethyl)-6-bromooxan-3-yl]oxyoxan-2-yl]methyl acetate

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:4753-07-5 SDS

4753-07-5Relevant articles and documents

Synthesis and galectin-binding activities of mercaptododecyl glycosides containing a terminal β-galactosyl group

Murakami, Teiichi,Yoshioka, Kyoko,Sato, Yukari,Tanaka, Mutsuo,Niwa, Osamu,Yabuki, Soichi

, p. 1265 - 1269 (2011)

Mercaptododecyl glycosides containing a terminal β-galactosyl group were prepared from d-galactose or from d-lactose via hexa-O-acetyl-lactal (10) as a key intermediate. Interactions of these glycolipids (5 kinds) and galectins (β-galactoside binding lectins, 6 species) were evaluated by surface plasmon resonance (SPR) method. High binding responses were observed for the lactoside, 2-deoxy-lactoside, and lactosaminide with some galectins (Gal-3, -4, -8), whereas the galactoside and 2,3-dideoxy-lactoside showed low binding activities.

Glysosylation of nucleophiles on ion-exchange resin: A new synthesis of dibenzyl glycosyl phosphates

Nazarova,Shpirt,Orlova,Kononov

, p. 1202 - 1204 (2015)

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Halogenation and anomerization of glycopyranoside by TESH/bromine and BHQ/bromine

Xu, Lai,Luo, Chin-Hung,Chen, Chien-Sheng

, p. 315 - 321 (2020/07/13)

Treatment of peracetylated glycosides and β-isopropyl glycosides with halogen in the presence of TESH and BHQ has been found to result in the halogenation and the anomerization, respectively. Peracetylatedglycosides treaded with I2/TESH or Br2/TESH leading tothe formation of corresponding glycosyl halides, and b-isopropyl glycosidesreacted with Br2/BHQ resulting in the formation of a-glycosides. The anomerizationof glycosidic bond was considered to be catalyzed by in situ formation of hydrogenbromide from the mixing of Br2/BHQ.

A Sweet H2S/H2O2Dual Release System and Specific Protein S-Persulfidation Mediated by Thioglucose/Glucose Oxidase

Ni, Xiang,Li, Xiaolu,Shen, Tun-Li,Qian, Wei-Jun,Xian, Ming

, p. 13325 - 13332 (2021/09/03)

H2S and H2O2 are two redox regulating molecules that play important roles in many physiological and pathological processes. While each of them has distinct biosynthetic pathways and signaling mechanisms, the crosstalk between these two species is also known to cause critical biological responses such as protein S-persulfidation. So far, many chemical tools for the studies of H2S and H2O2 have been developed, such as the donors and sensors for H2S and H2O2. However, these tools are normally targeting single species (e.g., only H2S or only H2O2). As such, the crosstalk and synergetic effects between H2S and H2O2 have hardly been studied with those tools. In this work, we report a unique H2S/H2O2 dual donor system by employing 1-thio-β-d-glucose and glucose oxidase (GOx) as the substrates. This enzymatic system can simultaneously produce H2S and H2O2 in a slow and controllable fashion, without generating any bio-unfriendly byproducts. This system was demonstrated to cause efficient S-persulfidation on proteins. In addition, we expanded the system to thiolactose and thioglucose-disulfide; therefore, additional factors (β-galactosidase and cellular reductants) could be introduced to further control the release of H2S/H2O2. This dual release system should be useful for future research on H2S and H2O2.

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