α-2,3-Sialyltransferase from Pasteurella multocida

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

Sialyltransferase catalyzes the transfer of Neu5Ac from CMP-Neu5Ac as a donor substrate to the β-D-galactosyl-1,4-N-acetyl-D-glucosaminyl termini of acceptor molecules including glycoproteins, glycolipids, and oligosaccharides.

Sialyltransferase transfers Neu5Ac from CMP-Neu5Ac to the galactosyl terminus of acceptor molecules including glycoproteins, glycolipids, and oligosaccharides.

Sialyltransferases belongs to the glycosyltransferases family with the capability of catalyzing the transfer of N-acetylneuraminic acid residues. It is a multifunctional enzyme with α-2,3-sialyltransferase activity, α-2,6-sialyltransferase activity, sialidase activity, and trans-sialidase activity. It has a molar mass of 46.4 kDa, with pI, pH being 5.94 and 7.5-8.5 respectively.

One unit will catalyze the formation of 1.0 μmol Neu-5-Ac-α-2,3LacMU from CMP-Neu-5-Ac and Lac-β−OMU per minute at 37 °C at pH 8.0.

Lyophilized powder containing Tris-HCl and NaCl

Reconstitute the lyophilized powder with a volume of water in the range of 0.1 mL to 1 mL, to give a concentration in the range of 1 unit/mL (1 mL volume of water) to 10 units/mL (0.1 mL volume of water).