抗人 ST3GAL1 抗体对
01AB01354
ST3 beta-galactoside alpha-2,3-sialyltransferase 1 (ST3GAL1) is a type II membrane glycoprotein enzyme belonging to glycosyltransferase family 29, catalyzing the transfer of sialic acid from CMP-Neu5Ac to galactose-containing substrates, primarily on glycoproteins and glycolipids. Structurally, ST3GAL1 contains conserved disulfide bonds critical for maintaining its active conformation, with key residues involved in donor and acceptor substrate binding and catalysis. The enzyme is predominantly localized in the Golgi apparatus but can be proteolytically processed to a soluble form. Functionally, ST3GAL1 regulates terminal sialylation of O-glycans, influencing cell adhesion and signaling pathways. Dysregulation of ST3GAL1 is implicated in cancer progression, notably promoting cell migration, invasion, and epithelial-mesenchymal transition (EMT) in ovarian and prostate cancers. It also contributes to tumor immune evasion by synthesizing sialoglycans that modulate the tumor microenvironment and confer resistance to chemotherapy agents like paclitaxel.
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技术参数
- 靶点基因名
- ST3GAL1
- 基因别名
- SIAT4; SIAT4A
- 蛋白别名
- ST3 beta-galactoside alpha-2,3-sialyltransferase 1; ST3GAL1
- UniProt
- Q11201
- 物种
- Human
产品详情
- 靶点名称
- ST3GAL1
- 蛋白名称
- ST3 beta-galactoside alpha-2,3-sialyltransferase 1
- 蛋白别名
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2; 3-sialyltransferase 1; Alpha 2; 3-ST 1; Beta-galactoside alpha-2; 3-sialyltransferase 1; Gal-NAc6S; Gal-beta-1; 3-GalNAc-alpha-2; 3-sialyltransferase; Monosialoganglioside sialyltransferase; SIATFL; ST3Gal I; ST3GalI; ST3GalA.1; ST3O; Sialyltransferase 4A; SIAT4-A
- 靶点基因名
- ST3GAL1
- 基因别名
- SIAT4; SIAT4A
- UniProt
- Q11201
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
ST3 beta-galactoside alpha-2,3-sialyltransferase 1 (ST3GAL1) is a type II membrane glycoprotein enzyme belonging to glycosyltransferase family 29, catalyzing the transfer of sialic acid from CMP-Neu5Ac to galactose-containing substrates, primarily on glycoproteins and glycolipids. Structurally, ST3GAL1 contains conserved disulfide bonds critical for maintaining its active conformation, with key residues involved in donor and acceptor substrate binding and catalysis. The enzyme is predominantly localized in the Golgi apparatus but can be proteolytically processed to a soluble form. Functionally, ST3GAL1 regulates terminal sialylation of O-glycans, influencing cell adhesion and signaling pathways. Dysregulation of ST3GAL1 is implicated in cancer progression, notably promoting cell migration, invasion, and epithelial-mesenchymal transition (EMT) in ovarian and prostate cancers. It also contributes to tumor immune evasion by synthesizing sialoglycans that modulate the tumor microenvironment and confer resistance to chemotherapy agents like paclitaxel.