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A0167

Sigma-Aldrich

Galacto-N-biose

Synonyme(s) :

β-D-Gal-(1→3)-D-GalNAc, 2-Acetamido-2-deoxy-3-O-β-D-galactopyranosyl-D-galactopyranose, T Antigen

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About This Item

Formule empirique (notation de Hill):
C14H25NO11
Numéro CAS:
20972-29-6
Poids moléculaire :
383.35
Numéro MDL:
MFCD00063995
Code UNSPSC :
12352201
ID de substance PubChem :
24890406
Nomenclature NACRES :
NA.25

Pureté

≥98% (TLC)

Forme

powder

Technique(s)

thin layer chromatography (TLC): suitable

Température de stockage

−20°C

Chaîne SMILES 

CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@H](O)[C@@H]1O[C@@H]2O[C@H](CO)[C@H](O)[C@H](O)[C@H]2O

InChI

1S/C14H25NO11/c1-4(18)15-7-12(9(20)6(3-17)24-13(7)23)26-14-11(22)10(21)8(19)5(2-16)25-14/h5-14,16-17,19-23H,2-3H2,1H3,(H,15,18)/t5-,6-,7-,8+,9+,10+,11-,12-,13-,14+/m1/s1

Clé InChI

HMQPEDMEOBLSQB-UFLFEMAHSA-N

Application

Galacto-N-biose, a component of the galacto-N-biose/lacto-N-biose metabolic pathway, is used as a substrate to identify, differentiate and characterize enzymes such as N-acetylglucosaminyltransferase(s), fucosyl- and sialyltransferase(s), galactosidase(s) and galacto-N-biose/lacto-N-biose I phosphorylase(s) (GLNBP). Galacto-N-biose is used in lectin inhibition studies.

Substrats

A substrate for N-acetylglucosaminyltransferase, fucosyl- and sialyltransferase, and galactosidase. Also used in lectin inhibition studies.

Autres remarques

To gain a comprehensive understanding of our extensive range of Disaccharides for your research, we encourage you to visit our Carbohydrates Category page.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

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S E Tollefsen et al.
The Journal of biological chemistry, 258(8), 5172-5176 (1983-04-25)
We have examined the carbohydrate binding specificity of the B4 lectin from Vicia villosa seeds. The B4 lectin agglutinates Tn-exposed erythrocytes specifically and binds to these erythrocytes (1.4 X 10(6) sites/cell) with an association constant of 4.2 X 10(7) M-1.
D Williams et al.
The Journal of biological chemistry, 255(23), 11253-11261 (1980-12-10)
The preceding paper (Williams, D., and Schachter, H. (1980) J. Biol. Chem. 255, 0000-0000) described a novel N-acetylglucosaminyltransferase in canine submaxillary gland microsomes which catalyzed the incorporation of GlcNAc into mucin acceptors. We show in the present report that the
T A Beyer et al.
The Journal of biological chemistry, 255(11), 5373-5379 (1980-06-10)
The acceptor substrate specificity and kinetic properties of the purified porcine submaxillary beta-galactoside alpha 1 leads to 2 fucosyltransferase have been examined. The transferase forms the Fuc alpha 1 leads to 2Gal linkage with oligosaccharides, glycoproteins, and glycolipids which contain
J I Rearick et al.
The Journal of biological chemistry, 254(11), 4444-4451 (1979-06-10)
The substrate requirements, linkage specificity, and kinetic mechanism of a pure sialyltransferase from porcine submaxillary glands have been examined. The enzyme transfers sialic acid from the donor nucleotide, CMP-NeuAc, into the sequence NeuAcalpha2 leads to 3Galbeta1 leads to 3GalNAc, which
The purification and properties of beta-galactosidase from bovine testes.
J J Distler et al.
The Journal of biological chemistry, 248(19), 6772-6780 (1973-10-10)
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