Anti-GALNT10 Antibody

Protein glycosylation is an important biological process that is carried out by a large family of glycosyltransferases that catalyze the synthesis of oligosaccharides and glycoconjugates. Polypeptide GalNAc transferases initiate the synthesis of mucin-type oligosaccharides by transferring GalNAc from UDP-GalNAc to the hydroxyl group of either a serine or threonine residue on the polypeptide acceptor. Polypeptide galactoaminyltransferase 10 (GALNT10) belongs to the polypeptide N-acetylgalactosaminyl-transferase (pp-GalNAc-T) protein family. Following expression in insect cells, recombinant GALNT10 showed significant GalNAcT activity toward mucin-derived peptides, and it utilized both non-glycosylated and glycosylated peptide substrates. GALNT10 mRNA is highly expressed in several distinct hypothalamic, thalamic, and amygdaloid nuclei in mouse brain. At least four isoforms of GALNT10 are known to exist.

GALNT10 antibody was raised against an 18 amino acid synthetic peptide near the carboxy terminus of human GALNT10. The immunogen is located within amino acids 530 - 580 of GALNT10.

Widely expressed. Expressed at high level in small intestine, and at intermediate levels in stomach, pancreas, ovary, thyroid gland and spleen. Weakly expressed in other tissues.

Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward Muc5Ac and EA2 peptide substrates.

GALNT10 antibody can be stored at 4°C for three months and -20°C, stable for up to one year. Avoid repeated freeze-thaw cycles. Antibodies should not be exposed to prolonged high temperatures.