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SAE0090

Sigma-Aldrich

Beta-galactoside alpha-2,6-sialyltransferase 1

≥300 units/mg protein, ST6GAL1 human recombinant, expressed in HEK 293 cells

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Synonym(s):
Alpha 2,6-ST 1, B-cell antigen CD75, CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1, ST6Gal I, Sialyltransferase 1
Enzyme Commission number:

recombinant

expressed in HEK 293 cells

assay

≥95% (The specific activity of ST6Gal I is measured by its ability to transfer sialic acid from CMP-NANA to asialofetuin., SDS-PAGE)

form

lyophilized powder

specific activity

≥300 units/mg protein

shipped in

ambient

storage temp.

−20°C

General description

Recombinant human Beta-galactoside alpha-2,6-sialyltransferase 1 (ST6Gal I) is expressed in human HEK 293 cells as a glycoprotein with a calculated molecular mass of 43.5 kDa (amino acids 27-406). The DTT-reduced protein migrates as a ~50 kDa polypeptide on SDS-PAGE due to glycosylation. This protein is manufactured in human cells, with no serum. The human cells expression system allows human-like glycosylation and folding, and often supports higher specific activity of the protein. The protein is produced with no artificial tags.

Biochem/physiol Actions

ST6Gal I catalyzes the transfer of CMP-N-acetylneuraminate (CMP-sialic acid, CMP-NANA) to the β-D-galactosyl-1,4-N-acetyl-D-glucosaminyl termini on glycoproteins. Sialic acids are distributed in a variety of glycolipids and glycoproteins.1 The sialic acid that is added to a galactose (Gal) can be bound either to the hydroxyl attached to carbon-3 of Gal to form an α-2,3 glycosidic linkage, or to the hydroxyl group attached to carbon-6 to form an α-2,6 glycosidic linkage.1 ST6Gal I generates a α-2,6 linkage of sialic acid on the non-reducing, terminal Galβ1 4GlcNAc residues of oligosaccharides and glycoconjugates.2

Terminal sialylation has been shown to decrease Fcγ receptor binding and increase anti-inflammatory activity,3 as well as antibody-dependent cellular cytotoxicity in different studies by reduced binding of sialylated antibody towards FcγRIIIa.4-5

This recombinant ST6Gal I product can be used to study the mode of action of the enzyme, as well as its potential inhibitors. It can also be used as a glycoengineering tool to modify glycoproteins in vitro.

CMP-N-acetylneuraminate (CMP-sialic acid, CMP-NANA) to the β-D-galactosyl-1,4-N-acetyl-D-glucosaminyl termini on glycoproteins.
Sialic acids are distributed in a variety of glycolipids and glycoproteins. The sialic acid that is added to a galactose (Gal) can be bound either to the hydroxyl attached to carbon-3 of Gal to form an α-2,3 glycosidic linkage, or to the hydroxyl group attached to carbon-6 to form an α-2,6 glycosidic linkage. ST6Gal I generates a α-2,6 linkage of sialic acid on the non-reducing, terminal Galβ1 4GlcNAc residues of oligosaccharides and glycoconjugates.

Terminal sialylation has been shown to decrease Fcγ receptor binding and increase anti-inflammatory activity, as well as antibody-dependent cellular cytotoxicity in different studies by reduced binding of sialylated antibody towards FcγRIIIa.

Unit Definition

One unit is defined as the amount of enzyme required to transfer 1.0 nanomole of sialic acid from CMP-NANA to asialofetuin per minute at pH 6.0, 37oC.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Articles

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

Enzymatic glycosyltransferase specificity challenges the one enzyme-one linkage concept.

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