抗人 GALNT10 抗体对
01AB01493
Polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10) is an enzyme that catalyzes the initial step in O-linked oligosaccharide biosynthesis, transferring N-acetyl-D-galactosamine from UDP-GalNAc to serine or threonine residues on polypeptide acceptors. It belongs to the family of GalNAc polypeptide N-acetylgalactosaminyltransferases and is involved in the synthesis of mucin-type oligosaccharides. GALNT10 is a type II membrane protein localized to the Golgi apparatus and exhibits metal ion binding properties. The enzyme has increased catalytic activity toward glycosylated peptides compared to non-glycosylated peptides. In terms of disease associations, GALNT10 has been implicated in cancer progression, particularly in gastric cancer where it promotes proliferation and metastasis while reducing 5-fluorouracil sensitivity by activating HOXD13. Additionally, alterations in GALNT10 expression have been observed in response to various chemical exposures, suggesting its potential role in environmental toxicology.
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技术参数
- 靶点基因名
- GALNT10
- 蛋白别名
- polypeptide N-acetylgalactosaminyltransferase 10; GALNT10
- UniProt
- Q86SR1
- 物种
- Human
产品详情
- 靶点名称
- GALNT10
- 蛋白名称
- polypeptide N-acetylgalactosaminyltransferase 10
- 蛋白别名
- Polypeptide N-acetylgalactosaminyltransferase 10; Polypeptide GalNAc transferase 10; GalNAc-T10; pp-GaNTase 10; Protein-UDP acetylgalactosaminyltransferase 10; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
- 靶点基因名
- GALNT10
- UniProt
- Q86SR1
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10) is an enzyme that catalyzes the initial step in O-linked oligosaccharide biosynthesis, transferring N-acetyl-D-galactosamine from UDP-GalNAc to serine or threonine residues on polypeptide acceptors. It belongs to the family of GalNAc polypeptide N-acetylgalactosaminyltransferases and is involved in the synthesis of mucin-type oligosaccharides. GALNT10 is a type II membrane protein localized to the Golgi apparatus and exhibits metal ion binding properties. The enzyme has increased catalytic activity toward glycosylated peptides compared to non-glycosylated peptides. In terms of disease associations, GALNT10 has been implicated in cancer progression, particularly in gastric cancer where it promotes proliferation and metastasis while reducing 5-fluorouracil sensitivity by activating HOXD13. Additionally, alterations in GALNT10 expression have been observed in response to various chemical exposures, suggesting its potential role in environmental toxicology.