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Merck

S2076

Sigma-Aldrich

α-2,6-Sialyltransferase from Photobacterium damsela

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

Sinónimos:

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

Comisión internacional de enzimas:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

recombinante

expressed in E. coli BL21

Nivel de calidad

Formulario

lyophilized powder

actividad específica

≥5 units/mg protein

mol peso

56.8 kDa

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

Descripción general

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

Aplicación

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

Acciones bioquímicas o fisiológicas

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). Bacterial α(2,6)-STs possesses broader acceptor substrate specificity when compared to eukaryotic α(2,6)-STs.

Definición de unidad

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.

Forma física

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

Nota de análisis

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).

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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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
Chompunuch Boonarkart et al.
Journal of medical virology, 84(3), 380-385 (2012-01-17)
A case of unusually high severity of influenza pneumonia leading to acute respiratory distress syndrome and death was investigated. This was a previously a healthy 28-year-old man with no underlying conditions, admitted to a hospital during the first wave of
N Li et al.
Acta virologica, 55(2), 147-153 (2011-06-23)
Human influenza viruses are major concern as the leading cause of global pandemics. In infecting cells, they preferentially bind to sialyloligosaccharides containing terminal N-acetyl sialic acid linked to galactose by an α-2,6-linkage (NeuAcα2,6Gal). The amount of NeuAcα2,6Gal in Vero cells
Adam W Barb et al.
Biochemistry, 51(22), 4618-4626 (2012-05-12)
The terminal carbohydrate residues of the N-glycan on the immunoglobulin G (IgG) fragment crystallizable (Fc) determine whether IgG activates pro- or anti-inflammatory receptors. The IgG Fc alone becomes potently anti-inflammatory upon addition of α2-6-linked N-acetylneuraminic acid residues to the N-glycan
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)

Artículos

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

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

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

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

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