Sialyltransferases are enzymes that transfer sialic acid to nascent oligosaccharide. Each sialyltransferase is specific for a particular sugar substrate. Sialyltransferases add sialic acid to the terminal portions of the sialylated glycolipids (gangliosides) or to the N-or O-linked sugar chains of glycoproteins. Sialyltransferases belong to glycosyltransferase family 29 (CAZY GT_29) which use a nucleotide monophosphosugar as the donor (CMP-NeuA) instead of a nucleotide diphosphosugar. Sialyltransferase transfers Neu5Ac from CMP-Neu5Ac to the galactosyl terminus of acceptor molecules including glycoproteins, glycolipids, and oligosaccharides.
α-Sialyltransferase, Recombinant (Photobacterium damsela)
Highly active α2-6 sialyltransferase has been used to prepare high levels of disialylated fragment crystals.
Supplied as a lyophilized powder containing Tris-HCl and NaCl.
Enzyme Commission Number
> 5 units/mg protein
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.
Store the product at –20 °C. It remains active for at least 1 year when stored properly.
Reconstitute the lyophilized powder with water to ~5 mg/mL. Solutions can be stored at 2–8°C for 1–2 months after reconstitution. They can also be aliquoted and frozen at –70°C or –20°C for 1 year. Multiple freeze-thaw cycles should be avoided.
α(2,6)-Sialyltransferase; Beta-galactoside alpha-2,6-sialyltransferase; Beta-galactosamide alpha-2,6-sialyltransferase; CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase; ST6Gal1; EC 188.8.131.52