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.
Anti-GALNT10 antibody was prepared from whole rabbit serum produced by repeated immunizations with a 16 amino acid synthetic peptide near the N-terminus of human GALNT10.
来源宿主
Rabbit
反应性
H. sapiens (Human); Mus musculus (Mouse); Rattus (Rat)
保存建议
Store vial at -20° C prior to opening. Aliquot contents and freeze at -20° C or below for extended storage. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4° C as an undiluted liquid. Dilute only prior to immediate use.
