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BENZYL 2-ACETAMIDO-2-DEOXY-3-O-BETA-D-GALACTOPYRANOSYL-ALPHA-D-GALACTOPYRANOSIDE is a complex carbohydrate derivative with a molecular structure that features a benzyl group and two sugar moieties, specifically a 2-acetamido-2-deoxy-3-O-beta-D-galactopyranosyl and an alpha-D-galactopyranoside. It is a white powder and is known for its role as a substrate and inhibitor in various biochemical processes.

3554-96-9

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3554-96-9 Usage

Uses

Used in Enzyme Research:
BENZYL 2-ACETAMIDO-2-DEOXY-3-O-BETA-D-GALACTOPYRANOSYL-ALPHA-D-GALACTOPYRANOSIDE is used as a substrate for N-acetyl-D-glucosaminyltransferase, an enzyme involved in the biosynthesis of complex carbohydrates. This application is crucial for studying the enzyme's function and its role in carbohydrate synthesis.
Used in Glycosylation Inhibition:
BENZYL 2-ACETAMIDO-2-DEOXY-3-O-BETA-D-GALACTOPYRANOSYL-ALPHA-D-GALACTOPYRANOSIDE also serves as an inhibitor of 1-3-galactotransferase, an enzyme that catalyzes the transfer of galactose to specific acceptor molecules. This inhibition property is valuable for investigating the enzyme's role in glycosylation processes and its potential impact on various biological functions.
Used in Biochemical Synthesis:
In the field of biochemistry, BENZYL 2-ACETAMIDO-2-DEOXY-3-O-BETA-D-GALACTOPYRANOSYL-ALPHA-D-GALACTOPYRANOSIDE is used as a substrate for UDP-GlcNAc:Gal1-beta-3GalNAc(GlcNAc-GalNAc)-6-beta-GlcNAc transferase and sialyltransferase. These enzymes are involved in the synthesis of complex carbohydrates and sialic acid-containing molecules, which are essential components of various biological systems.
Used in Pharmaceutical Industry:
BENZYL 2-ACETAMIDO-2-DEOXY-3-O-BETA-D-GALACTOPYRANOSYL-ALPHA-D-GALACTOPYRANOSIDE is used as a key intermediate in the synthesis of various pharmaceutical compounds, particularly those targeting carbohydrate-based drug development. Its unique structure allows for the creation of novel drug candidates with potential therapeutic applications.
Used in Diagnostics:
BENZYL 2-ACETAMIDO-2-DEOXY-3-O-BETA-D-GALACTOPYRANOSYL-ALPHA-D-GALACTOPYRANOSIDE can also be employed in the development of diagnostic tools, as its interaction with specific enzymes and receptors can be utilized to detect and monitor certain biological processes or conditions related to carbohydrate metabolism and glycosylation.

Check Digit Verification of cas no

The CAS Registry Mumber 3554-96-9 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 3,5,5 and 4 respectively; the second part has 2 digits, 9 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 3554-96:
(6*3)+(5*5)+(4*5)+(3*4)+(2*9)+(1*6)=99
99 % 10 = 9
So 3554-96-9 is a valid CAS Registry Number.
InChI:InChI=1/C21H31NO11/c1-10(25)22-14-19(33-21-18(29)17(28)15(26)12(7-23)32-21)16(27)13(8-24)31-20(14)30-9-11-5-3-2-4-6-11/h2-6,12-21,23-24,26-29H,7-9H2,1H3,(H,22,25)/t12?,13?,14-,15-,16-,17-,18-,19+,20-,21-/m0/s1

3554-96-9SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 13, 2017

Revision Date: Aug 13, 2017

1.Identification

1.1 GHS Product identifier

Product name Benzyl 2-Acetamido-2-deoxy-3-O-(β-D-galactopyranosyl) α-D-galactopyranoside

1.2 Other means of identification

Product number -
Other names N-[(2S,3R,4R,5R,6R)-5-hydroxy-6-(hydroxymethyl)-2-phenylmethoxy-4-[(2R,3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-3-yl]acetamide

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:3554-96-9 SDS

3554-96-9Relevant academic research and scientific papers

Facile one-step syntheses of modified O-glycoprotein Galβ1-3GalNAc structures by transglycosylation employing three β-galactosidases from bovine testes, Xanthomonas manihotis, and Bacillus circulans

Kroeger, Lars,Thiem, Joachim

, p. 717 - 722 (2005)

Natural O-glycoproteins such as the Thomsen-Friedenreich antigen or gangliosides contain the motif Galβ1-3GalNAc as an important disaccharide with significant biologic activity. The arrangement of spatial functionalities in this structure are of particular interest with regard to the development of potential leads en route to pharmaceuticals. Therefore, it was desired to obtain access to a range of modified derivatives of the aforementioned motif paying particular attention to introducing specific deoxy functions instead of hydroxyl groups. Copyright Taylor & Francis, Inc.

Characterization of the Immobilized β-Galactosidase C from Bacillus circulans and the Production of β(1→3)-linked Disaccharides

Naundorf, Andreas,Caussette, Mylene,Ajisaka, Katsumi

, p. 1313 - 1317 (1998)

A recombinant β-galactosidase, which was obtained from the β-galactosidase C gene of Bacillus circulans and cleaves the non-reducing end galactosyl residue of β(1→3)-linkages selectively, was immobilized using CNBr-Sepharose. Although the effect of pH was not changed by the immobilization, the thermostability and stability in the presence of DMF were increased. Optimization of the transglycosylation using para-nitrophenyl β-D-galactopyranoside as a donor and benzyl-α-D-N-acetylgalactosaminide as an acceptor afforded a β(1→3)-linked disaccharide derivative with 62% molar yield in a gram scale synthesis. Using the methyl-analogue as an acceptor, 53% of the acceptor was converted to the respective β(1→3)-disaccharide.

Fluorescence activated cell sorting as a general ultra-high-throughput screening method for directed evolution of glycosyltransferases

Yang, Guangyu,Rich, Jamie R.,Gilbert, Michel,Wakarchuk, Warren W.,Feng, Yan,Withers, Stephen G.

experimental part, p. 10570 - 10577 (2010/09/17)

Glycosyltransferases (GTs) offer very attractive approaches to the synthesis of complex oligosaccharides. However, the limited number of available GTs, together with their instability and strict substrate specificity, have severely hampered the broad application of these enzymes. Previous attempts to broaden the range of substrate scope and to increase the activity of GTs via protein engineering have met with limited success, partially because of the lack of effective high-throughput screening methods. Recently, we reported an ultra-high-throughput screening method for sialyltransferases based on fluorescence-activated cell sorting (Aharoni et al. Nat. Methods 2006, 3, 609-614). Here, we considerably improve this method via the introduction of a two-color screening protocol to minimize the probability of false positive mutants and demonstrate its generality through directed evolution of a neutral sugar transferase, β-1,3-galactosyltransferase CgtB. A variant with broader substrate tolerance than the wild-type enzyme and 300-fold higher activity was identified rapidly from a library of >107 CgtB mutants. Importantly, the variant effected much more efficient synthesis of G M1a and asialo GM1 oligosaccharides, the building blocks of important therapeutic glycosphingolipids, than did the parent enzyme. This work not only establishes a new methodology for the directed evolution of galactosyltransferases, but also suggests a powerful strategy for the screening of almost all GT activities, thereby facilitating the engineering of glycosyltransferases.

Fibrinogen-coated particles for therapeutic use

-

, (2008/06/13)

The invention provides a particle comprising fibrinogen bound on the surface of an albumin matrix, wherein said particle is capable of coaggregation with platelet, and of aggregation in a solution containing soluble fibrinogen at a concentration of soluble fibrinogen not capable by it self of formation of a clot upon activation by thrombin.

Non-crosslinked protein particles for therapeutic and diagnostic use

-

, (2008/06/13)

Albumin particles in the nanometer and micrometer size range in an aqueous suspension are rendered stable against resolubilization without the aid of a crosslinking agent and without denaturation, by the incorporation of a stabilizing agent in the particle composition. Particles which are primarily albumin in the nanometer and micrometer size range in an aqueous suspension are rendered stable against resolublization by the incorporation of a reducing agent, oxidizing agent, hydrogen-accepting molecule, high molecular weight polymer, sulfur-containing ring compound or combinations thereof.

Non-crosslinked protein particles for therapeutic and diagnostic use

-

, (2008/06/13)

Albumin particles in the nanometer and micrometer size range in an aqueous suspension are rendered stable against resolubilization without the aid of a crosslinking agent and without denaturation, by the incorporation of hemoglobin in the particle composition. Particles which are primarily hemoglobin in the nanometer and micrometer size range in an aqueous suspension are rendered stable against aggregation by the incorporation of either albumin, surface active agents or gelatin.

Synthetic mucin fragments: benzyl 2-acetamido-6-O-(2-acetamido-2-deoxy-beta- D-glucopyranosyl)-2-deoxy-3-O-beta-D-galactopyranosyl-alpha-D- galactopyranoside and benzyl 2-acetamido-6-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)- 3-O-[6-O-(2-acetamido-2-d

Piskorz,Abbas,Matta

, p. 115 - 124 (2007/10/02)

Glycosylation of benzyl 2-acetamido-4,6-O-benzylidene-2-deoxy-alpha-D- galactopyranoside with 2,3,4,6-tetra-O-acetyl-alpha-D-galactopyranosyl bromide, catalyzed by mercuric cyanide, afforded benzyl-2-acetamido-4,6-O-benzylidene-2-deoxy-3- O-(2,3,4,6-tetra

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