GALNT10 Mouse anti-Human, Clone: OTI2A12, Invitrogen
Mouse Monoclonal Antibody
Manufacturer: Invitrogen MA527144
DescriptionProtein 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, recombit 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.
|PBS with 1% BSA, 50% glycerol and 0.02% sodium azide; pH 7.3|
|GALNACT10, PPGALNACT10, PPGANTASE10; GalNAc transferase 10; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10; polypeptide N-acetylgalactosaminyltransferase 10|
|-20° C, Avoid Freeze/Thaw Cycles|
|Immunohistochemistry (Paraffin), Western Blot|
|Human recombit protein fragment corresponding to amino acids 1-318 of GALNT10 produced in E.coli|
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