Anti-B3GNT8 Antibody Picoband® Fluoro647 Conjugated

B3GNT8 is a galactosyltransferase involved in the synthesis of poly-N-acetyllactosamine (polyLacNAc), a linear chain of repeating LacNAc units made up of galactose (Gal) and N-acetylglucosamine (GlcNAc) with the structure (Gal-beta-1-4-GlcNAc-beta-1-3) n. By genomic sequence analysis, the B3GNT8 gene is mapped to chromosome 19q13.2. It was showed that a soluble form of B3GNT8 overexpressed by transfected HEK293 cells selectively transferred GlcNAc from UDP-GlcNAc to the nonreducing terminus of Gal-beta-1-4-GlcNAc-alpha-p-nitrophenyl phosphate and to lactoside-alpha-benzoyl. It did not utilize keratan sulfates or polylactosamine oligosaccharide as substrate. B3GNT8 activity required Mn (2+) and showed less efficiency with Co (2+) . The pH optimum was between 7 and 7.5. B3GNT8 also transferred GlcNAc onto alpha-1-acid glycoprotein and ovomucoid, which possess tetraantennary complex type and pentaantennary complex type N-glycans. With a tetraantennary N-glycan substrate, B3GNT8 appeared to prefer the beta-1-2 branch over the beta-1-6 branch. When overexpressed in HCT15 human colon cancer cells, B3GNT8 increased cell surface expression of both polyLacNAc and beta-1-6-branched N-glycans.

UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 8; BGnT-8; Beta-1,3-Gn-T8; Beta-1,3-N-acetylglucosaminyltransferase 8; Beta3Gn-T8;2.4.1.-; B3GNT8 ; B3GALT7 , BGALT15

Highly expressed in small intestine, pancreas, spleen, bone marrow, lung, throat, and ileum, and weakly in fetal brain, cerebellum, heart, liver, tongue, breast, uteri, and testis. Not detected in colon. Differentially expressed in human tumor cell lines. .

Beta-1,3-N-acetylglucosaminyltransferase that plays a role in the elongation of specific branch structures of multiantennary N-glycans. Has strong activity towards tetraantennary N-glycans and 2,6 triantennary glycans. .

1. Ishida, H., Togayachi, A., Sakai, T., Iwai, T., Hiruma, T., Sato, T., Okubo, R., Inaba, N., Kudo, T., Gotoh, M., Shoda, J., Tanaka, N., Narimatsu, H. A novel beta-1,3-N-acetylglucosaminyltransferase (beta-3Gn-T8), which synthesizes poly-N-acetyllactosamine, is dramatically upregulated in colon cancer. FEBS Lett. 579: 71-78, 2005. 2. Seko, A., Yamashita, K. Activation of beta-1,3-N-acetylglucosaminyltransferase-2 (beta-3Gn-T2) by beta-3Gn-T8: possible involvement of beta-3Gn-T8 in increasing poly-N-acetyllactosamine chains in differentiated HL-60 cells. J. Biol. Chem. 283: 33094-33100, 2008.