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.
α-2,3-Sialyltransferase is used for targeted, in vitro sialylation of glycoproteins, which are not, or not fully sialylated.
clear, colorless to slightly colored solution.
α-2,3-Sialyltransferase is used for in vitro sialylation of all Galβ1-4GlcNAc units on glycoproteins, such as monoclonal antibodies (MABs). Clear colorless to slightly colored solution. 50 mM MES, 200 mM NaCl, pH 6.4 ± 0.1 at 4°C. Easily increase glycosyslation homogeneity and be less dependent on certain cell lines and time-consuming optimization of fermentation conditions. Obtain higher yields of glycosylated proteinby optimization of your fermentation process for high yield instead of glycosylation patterns. Benefit from Roche quality and manufacturing capabilities: Glycotransferases are animal-free, available from small to large scale and in GMP quality on request.
> 80 U/µg (1 Unit = pmol / min, using 10 µg enzyme in Sialyltransferase activity assay)
50 mM MES, 200 mM NaCl, pH 6.4 ± 0.1 at +4°C.
at -15°C to -25°C: within specification range for 12 months.
α (2,3)-Sialyltransferase; Beta-galactoside alpha-2,3-sialyltransferase; Beta-galactosamide alpha-2,3-sialyltransferase; CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase