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S2076

Sigma-Aldrich

α-2,6-Sialyltransferase from Photobacterium damsela

recombinant, expressed in E. coli BL21, ≥5 units/mg protein

Synonyme(s) :

β-Galactoside α-2,6-sialyltransferase, CMP-N-Acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine α-2,6-N-acetylneuraminyltransferase

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About This Item

Numéro de classification (Commission des enzymes):
2.4.99.1 (BRENDA, IUBMB)
Numéro MDL:
MFCD00132245
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Le tarif et la disponibilité ne sont pas disponibles actuellement.

Produit recombinant

expressed in E. coli BL21

Niveau de qualité

200

Forme

lyophilized powder

Activité spécifique

≥5 units/mg protein

Poids mol.

56.8 kDa

Conditions d'expédition

dry ice

Température de stockage

−20°C

Description générale

Human ST6Gal-I (β-galactoside α-2,6-sialyltransferase 1) is a member of the CAZy family GT29.[1]

Application

α-2,6-Sialyltransferase from Photobacterium damsela has been used in resialylation and restoration of sialic acids (SAs) in HRT-18G cells.[2]
Highly active α2-6 sialyltransferase has been used to prepare high levels of disialylated fragment crystals. [3]

Actions biochimiques/physiologiques

Sialyltransferase transfers Neu5Ac from CMP-Neu5Ac to the galactosyl terminus of acceptor molecules including glycoproteins, glycolipids, and oligosaccharides.
The terminal step of complex N-glycan biosynthesis is catalysed by α-2,6-sialyltransferase (STs).[1] Bacterial α(2,6)-STs possesses broader acceptor substrate specificity when compared to eukaryotic α(2,6)-STs.[4]

Définition de l'unité

One unit will catalyze the formation of 1 μmol Neu-5-Ac-α-2,6-LacMU from CMP-Neu-5-Ac and Lac-β−OMU per minute at 37 °C at pH 8.0.

Forme physique

Supplied as a lyophilized powder containing Tris-HCl and NaCl.

Remarque sur l'analyse

Enzymatic activity assays are performed in Tris-HCl buffer (100 mM, pH 8.0) containing CMP-Neu-5-Ac (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).

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

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Certificats d'analyse (COA)

Lot/Batch Number
0000415709
0000415709
0000356578
0000356578
0000305184

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Consulter la Bibliothèque de documents

Nageswari Yarravarapu et al.
Bioconjugate chemistry, 33(5), 781-787 (2022-04-20)
Glycan binding often mediates extracellular macromolecular recognition events. Accurate characterization of these binding interactions can be difficult because of dissociation and scrambling that occur during purification and analysis steps. Use of photocrosslinking methods has been pursued to covalently capture glycan-dependent
Enhanced Bacterial alpha (2, 6)-Sialyltransferase Reaction through an Inhibition of Its Inherent Sialidase Activity by Dephosphorylation of Cytidine-5'-Monophosphate
Kang JY, et al.
PLoS ONE, 10(7), e0133739-e0133739 (2015)
High-quality production of human alpha-2, 6-sialyltransferase in Pichia pastoris requires control over N-terminal truncations by host-inherent protease activities
Ribitsch D, et al.
Microbial cell factories, 13, 138-138 (2014)
Miyako Nakano et al.
Molecular & cellular proteomics : MCP, 10(11), M111-M111 (2011-08-24)
Resistance to tubulin-binding agents used in cancer is often multifactorial and can include changes in drug accumulation and modified expression of tubulin isotypes. Glycans on cell membrane proteins play important roles in many cellular processes such as recognition and apoptosis
Masayoshi Onitsuka et al.
Applied microbiology and biotechnology, 94(1), 69-80 (2011-12-30)
Improvement of glycosylation is one of the most important topics in the industrial production of therapeutic antibodies. We have focused on terminal sialylation with alpha-2,6 linkage, which is crucial for anti-inflammatory activity. In the present study, we have successfully cloned
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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

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