protein

ST6GALNAC2 Protein, Human (HEK293, His)

HY-P71332

10 μg;50 μg

140;420 USD

ST6GALNAC2 Protein, Human (HEK293, His)

proteins

HEK293

10 μg;50 μg

140;420 USD

The ST6GALNAC2 protein is an essential enzyme that catalyzes the transfer of N-acetylneuramidyl groups to glycan chains in glycoproteins. This glycosyltransferase shows a preference for N-acetylgalactosamine (GalNAc) residues that have been modified by the addition of galactose or galactose followed by the addition of sialic acid in an α-2,3 linkage. ST6GALNAC2 Protein, Human (HEK293, His) is the recombinant human-derived ST6GALNAC2 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of ST6GALNAC2 Protein, Human (HEK293, His) is 346 a.a., with molecular weight of ~44.0 kDa.

Human

ST6 N-Acetylgalactosaminide Alpha-2,6-Sialyltransferase 2 (ST6GALNAC2) is an enzyme that catalyzes the transfer of N-acetylneuraminyl groups onto glycan chains in glycoproteins. This sialyltransferase exhibits a preference for glycan structures where N-acetylgalactosamine (GalNAc) residues are already modified by the addition of galactose or galactose followed by sialic acid in alpha-2,3 linkage. The enzymatic activity of ST6GALNAC2 contributes to the addition of sialic acid residues to glycoproteins, modulating their functional properties and interactions. Sialylation is a crucial post-translational modification with implications in cell adhesion, immune response, and signaling. Understanding the substrate specificity of ST6GALNAC2 provides insights into its role in the intricate regulation of glycan structures and their impact on diverse cellular processes.

Alpha-N-Acetylgalactosaminide Alpha-2; 6-Sialyltransferase 2; GalNAc Alpha-2; 6-Sialyltransferase II; ST6GalNAc II; ST6GalNAcII; SThM; Sialyltransferase 7B; SIAT7-B; ST6GALNAC2; SIAT7B; SIATL1; STHM

Greater than 95% as determined by reducing SDS-PAGE.

Supplied as a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, 5 mM EDTA, 5% Trehalosen, pH 7.4.

Shipping with dry ice