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alpha-2,6-sialyltransferase
From
€580.00
From €39.2 per standard enzyme unit
Synonyms: β-Galactoside α-2,6-sialyltransferase, CMP-N-Acetylneuraminate:β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine α-2,6-N-acetylneuraminyltransferase
Unit definition (U) (standard enzyme unit): One unit is defined as the formation of 1 μmol Neu5Ac-α-2,6-lactose (6’SL) from CMP-Neu5Ac (1 mM) and lactose (1 mM) per minute at 37 °C at pH 8.0.
The enzyme is for research use only. Not for use in diagnostic procedures.
Quantity
Technical Specifications
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Description: |
This recombinant bacterial α-2,6-sialyltransferase (α2,6SiaT) is expressed in E. coli BL21(DE3) and is designed for sialylation of glycoproteins, glycolipids, and free glycans (including oligosaccharides). It catalyzes the transfer of sialic acid from CMP-Neu5Ac (or other CMPNeu5Ac analogues) to terminal galactose residues in a α-2,6 linkage. Compared to other known α2,6SiaTs, this enzyme has suppressed hydrolytic activities, resulting in enhanced synthesis |
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Molecular weight |
45 kDa |
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Expression host: |
E. coli BL21(DE3) |
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Purity: |
> 90 % (SDS-PAGE) |
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His-tag: |
Yes |
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Form: |
Lyophilized powder (MOPS and NaCl) |
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Reconstitution: |
Add 10–100 µL deionized water |
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Store at: |
-20 °C |
Enzymatic activity characterisation
• Donor substrate: CMP-Neu5Ac
• Acceptor substrate: Glycans with terminal galactose
• Reaction conditions: pH 6.5–8.0; 25–37 °C
• Transferase activity: α-2,6-sialyltransferase
• Hydrolytic activity: Trace
• Sialidase activity: Undetectable
Activity validation
The activity of the enzyme was validated on the following substrates
• Free G2F glycans (See more in the image session)
• Rituximab (in combination with β1,4-GalT)
Assay method: Capillary gel electrophoresis with laser-induced fluorescence
Application examples
• For the sialylation of a wide range of glycans: G2F, G2, lactose, LNT, LNnT, etc.
• For the sialylation of glycoproteins: Rituximab (in combination with β1,4-GalT),
• Erythropoietin (EPO) for terminal sialylation, Fc-fusion proteins for enhanced serum half-life
• Glycan arrays for binding studies
The enzyme is for research use only. Not for use in diagnostic procedures.
