抗人 SUMF1 抗体对
01AB01367
Sulfatase modifying factor 1 (SUMF1) is a glycosylated enzyme localized primarily in the endoplasmic reticulum (ER) and is essential for the post-translational activation of all eukaryotic sulfatases by converting a specific cysteine residue in their active site to C-alpha-formylglycine (FGly), a modification necessary for their catalytic activity. SUMF1 can also be secreted and subsequently taken up by cells, where it is trafficked back to the ER and remains functionally active, enhancing sulfatase activities in various tissues. Both glycosylated and non-glycosylated forms of SUMF1 can be secreted, but only the glycosylated form is efficiently internalized by cells through a receptor-mediated process. Mutations in the SUMF1 gene can disrupt FGly formation, leading to inactive sulfatases and causing multiple sulfatase deficiency (MSD), a rare lysosomal storage disorder characterized by the combined loss of function of all sulfatases, resulting in the accumulation of sulfated substrates and severe clinical symptoms.
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技术参数
- 靶点基因名
- SUMF1
- 蛋白别名
- sulfatase modifying factor 1; SUMF1
- UniProt
- Q8NBK3
- 物种
- Human
产品详情
- 靶点名称
- SUMF1
- 蛋白名称
- sulfatase modifying factor 1
- 蛋白别名
- Formylglycine-generating enzyme; FGE; C-alpha-formylglycine-generating enzyme 1; Sulfatase-modifying factor 1
- 靶点基因名
- SUMF1
- UniProt
- Q8NBK3
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Sulfatase modifying factor 1 (SUMF1) is a glycosylated enzyme localized primarily in the endoplasmic reticulum (ER) and is essential for the post-translational activation of all eukaryotic sulfatases by converting a specific cysteine residue in their active site to C-alpha-formylglycine (FGly), a modification necessary for their catalytic activity. SUMF1 can also be secreted and subsequently taken up by cells, where it is trafficked back to the ER and remains functionally active, enhancing sulfatase activities in various tissues. Both glycosylated and non-glycosylated forms of SUMF1 can be secreted, but only the glycosylated form is efficiently internalized by cells through a receptor-mediated process. Mutations in the SUMF1 gene can disrupt FGly formation, leading to inactive sulfatases and causing multiple sulfatase deficiency (MSD), a rare lysosomal storage disorder characterized by the combined loss of function of all sulfatases, resulting in the accumulation of sulfated substrates and severe clinical symptoms.