Accéder au contenu
Merck
Toutes les photos(2)

Key Documents

View All Documentation

S1951

Sigma-Aldrich

α-2,3-Sialyltransferase from Pasteurella multocida

recombinant, expressed in E. coli BL21, ≥2 units/mg protein

Synonyme(s) :

CMP-N-acetylneuraminate:β-D-galactoside α-(2,3)-N-acetylneuraminyltransferase

Se connecterpour consulter vos tarifs contractuels et ceux de votre entreprise/organisme
Toutes les photos(2)

About This Item

Numéro de classification (Commission des enzymes):
2.4.99.4 (BRENDA, IUBMB)
Numéro MDL:
MFCD00130470
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Produit recombinant

expressed in E. coli BL21

Niveau de qualité

200

Forme

lyophilized powder

Activité spécifique

≥2 units/mg protein

Poids mol.

46.4 kDa

Conditions d'expédition

dry ice

Température de stockage

−20°C

Description générale

Sialyltransferases belongs to the glycosyltransferases family with the capability of catalyzing the transfer of N-acetylneuraminic acid residues. It is a multifunctional enzyme with α-2,3-sialyltransferase activity, α-2,6-sialyltransferase activity, sialidase activity, and trans-sialidase activity. It has a molar mass of 46.4 kDa, with pI, pH being 5.94 and 7.5-8.5 respectively.

Actions biochimiques/physiologiques

Sialyltransferase catalyzes the transfer of Neu5Ac from CMP-Neu5Ac as a donor substrate to the β-D-galactosyl-1,4-N-acetyl-D-glucosaminyl termini of acceptor molecules including glycoproteins, glycolipids, and oligosaccharides.
Sialyltransferase transfers Neu5Ac from CMP-Neu5Ac to the galactosyl terminus of acceptor molecules including glycoproteins, glycolipids, and oligosaccharides.

Définition de l'unité

One unit will catalyze the formation of 1.0 μmol Neu-5-Ac-α-2,3LacMU from CMP-Neu-5-Ac and Lac-β−OMU per minute at 37 °C at pH 8.0.

Forme physique

Lyophilized powder containing Tris-HCl and NaCl

Notes préparatoires

Reconstitute the lyophilized powder with a volume of water in the range of 0.1 mL to 1 mL, to give a concentration in the range of 1 unit/mL (1 mL volume of water) to 10 units/mL (0.1 mL volume of water).

Remarque sur l'analyse

Enzymatic activity assays performed in Tris-HCl buffer (100 mM, pH 8.0) containing CMP-Neu-5Ac (1 mM) and Lac-β−OMU (1 mM) at 37°C for 30 min and analyzed using HPLC with a fluorescence detector (excitation at 325 nm and emission at 372 nm).

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H334

Conseils de prudence

P261 - P284 - P501

Classification des risques

Resp. Sens. 1

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

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

Déjà en possession de ce produit ?

Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Yoshimitsu Kakuta et al.
Glycobiology, 18(1), 66-73 (2007-10-27)
Sialyltransferases are a family of glycosyltransferases that catalyze the transfer of N-acetylneuraminic acid residues from cytidine monophosphate N-acetylneuraminic acid (CMP-NeuAc) as a donor substrate to the carbohydrate groups of glycoproteins and glycolipids as acceptor substrates. We determined the crystal structure
Sung-Wook Son et al.
Biochemical and biophysical research communications, 414(1), 159-164 (2011-09-29)
In this study we investigated for the first time the transcriptional regulation of pig Galβ1,3GalNAc α2,3-sialyltransferase (pST3Gal I) in response to TGF-β1 in porcine kidney PK-15 cells. The pST3Gal I gene was found to span about 90kb and to be
Vireak Thon et al.
Applied microbiology and biotechnology, 94(4), 977-985 (2011-11-15)
Pasteurella multocida (Pm) strain Pm70 has three putative sialyltransferase genes including Pm0188, Pm0508, and Pm1174. A Pm0188 gene homolog in Pm strain P-1059 encodes a multifunctional α2-3-sialyltransferase, PmST1, that prefers oligosaccharide acceptors. A Pm0508 gene homolog in the same strain
Lisheng Ni et al.
Biochemistry, 45(7), 2139-2148 (2006-02-16)
Sialyltransferases catalyze reactions that transfer a sialic acid from CMP-sialic acid to an acceptor (a structure terminated with galactose, N-acetylgalactosamine, or sialic acid). They are key enzymes that catalyze the synthesis of sialic acid-containing oligosaccharides, polysaccharides, and glycoconjugates that play
Vishwanath B Chachadi et al.
The international journal of biochemistry & cell biology, 43(4), 586-593 (2010-12-21)
Sialyl Lewis X is a tumor-associated antigen frequently found in the advanced cancers. However, the mechanism for the production of this cancer antigen is not entirely clear. The objective of this study is to examine whether epigenetics is involved in
Afficher tous les articles scientifiques apparentés

Articles

Glycosyltransferases: Tools for Synthesis and Modification of Glycans

Explore tools for glycosyltransferase synthesis and modification of glycans, such as glycosyltransferases and nucleotide sugar donors.

Glycosyltransferases: Tools for Synthesis and Modification of Glycans

Explore tools for glycosyltransferase synthesis and modification of glycans, such as glycosyltransferases and nucleotide sugar donors.

Glycosyltransferases: Tools for Synthesis and Modification of Glycans

Explore tools for glycosyltransferase synthesis and modification of glycans, such as glycosyltransferases and nucleotide sugar donors.

Glycosyltransferases: Tools for Synthesis and Modification of Glycans

Explore tools for glycosyltransferase synthesis and modification of glycans, such as glycosyltransferases and nucleotide sugar donors.

Afficher tout

Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..

Contacter notre Service technique