Human ST6 Gal Sialyltransferase 2/ST6GAL2 Alexa Fluor™ Plus 680-conjugated Antibody

ST6GAL2 (Sialyltransferase 2; also beta-galactoside alpha-2,6 Sialyltransferase 2) is a 60-62 kDa member of the glycosyltransferase 29 family of enzymes. It has restricted expression, likely being found in neurons and bronchial eipthelium. ST6GAL2 transfers sialic acid from CMP-Neu5Ac to a galactose that is linked to N‑Aceylglucosamine through a beta1-4 linkage (Gal beta1-4GlcNac). This transfer will occur when the target motif is found either on select glycoproteins or free oligosaccharides. Notably, the kinetics of this enzyme suggest additional biological functions other than sialic acid transfer. Human ST6GAL2 is a 529 amino acid (aa) type II transmembrane Golgi protein. It contains an 11 aa N‑terminal cytoplasmic region and a 497 aa luminal domain (aa 33-529). The luminal domain possesses an L motif that binds CMP-Sialic acid (aa 296-343), an S motif that binds CMP-Sialic acid and galactose (aa 444-458) and a VS motif that is involved with the enzyme's catalytic activity (aa 483-488). There is some evidence that ST6GAL2 may form homodimers. There is one splice variant that shows a 26 aa substitution for aa 441‑529. Over aa 243-529, human ST6GAL2 shares 88% aa sequence identity with mouse ST6GAL2.