人 FUT8 抗体对
01AB03404
Fucosyltransferase 8 (FUT8) is a Golgi-localized type II transmembrane glycoprotein that catalyzes core fucosylation, a critical post-translational modification involving the addition of fucose to the innermost GlcNAc residue of N-glycans. The enzyme features a complex domain structure, including a catalytic Rossmann fold and a unique C-terminal SH3 domain that regulates its activity, homodimerization, and interaction with ribophorin I. Core fucosylation by FUT8 is essential for the proper biological function of numerous glycoproteins. Clinically, dysregulated FUT8 activity is strongly implicated in cancer progression, where elevated core fucose levels promote tumor metastasis and signaling. Additionally, congenital deficiency of FUT8 leads to a rare disorder of glycosylation known as CDG-IIh, which is characterized by severe immunodeficiency, developmental delay, and failure to thrive. These roles highlight FUT8 as a fundamental regulator of glycoprotein maturation and a significant factor in both developmental biology and oncogenic pathology.
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技术参数
- 靶点基因名
- FUT8
- 蛋白别名
- fucosyltransferase 8; FUT8
- UniProt
- Q9BYC5
- 物种
- Human
产品详情
- 靶点名称
- FUT8
- 蛋白名称
- fucosyltransferase 8
- 蛋白别名
- Alpha-(1; 6)-fucosyltransferase; Alpha1-6FucT; Fucosyltransferase 8; GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1; 6-fucosyltransferase; GDP-fucose--glycoprotein fucosyltransferase; Glycoprotein 6-alpha-L-fucosyltransferase
- 靶点基因名
- FUT8
- UniProt
- Q9BYC5
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Fucosyltransferase 8 (FUT8) is a Golgi-localized type II transmembrane glycoprotein that catalyzes core fucosylation, a critical post-translational modification involving the addition of fucose to the innermost GlcNAc residue of N-glycans. The enzyme features a complex domain structure, including a catalytic Rossmann fold and a unique C-terminal SH3 domain that regulates its activity, homodimerization, and interaction with ribophorin I. Core fucosylation by FUT8 is essential for the proper biological function of numerous glycoproteins. Clinically, dysregulated FUT8 activity is strongly implicated in cancer progression, where elevated core fucose levels promote tumor metastasis and signaling. Additionally, congenital deficiency of FUT8 leads to a rare disorder of glycosylation known as CDG-IIh, which is characterized by severe immunodeficiency, developmental delay, and failure to thrive. These roles highlight FUT8 as a fundamental regulator of glycoprotein maturation and a significant factor in both developmental biology and oncogenic pathology.