
人 SSR1 抗体对
01AB02313
Signal sequence receptor subunit 1 (SSR1), also known as TRAP alpha, is a type I glycosylated membrane protein located in the endoplasmic reticulum (ER). It serves as the alpha subunit of the heterotetrameric translocon-associated protein (TRAP) complex, which is essential for the co-translational translocation of secretory and membrane proteins across the ER membrane. SSR1 functions as a membrane-bound chaperone that facilitates the proper folding of nascent polypeptides and contributes to calcium binding and the retention of ER-resident proteins. Its fundamental role in protein biogenesis is underscored by the fact that its loss leads to neonatal lethality and severe developmental defects. Clinically, dysregulated SSR1 expression has been linked to various malignancies, including diffuse large B-cell lymphoma and hypopharyngeal squamous cell carcinoma, where it may participate in oncogenic signaling axes.
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技术参数
- 靶点基因名
- SSR1
- 基因别名
- TRAPA
- 蛋白别名
- signal sequence receptor subunit 1; SSR1
- UniProt
- P43307
- 物种
- Human
产品详情
- 靶点名称
- SSR1
- 蛋白名称
- signal sequence receptor subunit 1
- 蛋白别名
- Translocon-associated protein subunit alpha; TRAP-alpha; Signal sequence receptor subunit alpha; SSR-alpha
- 靶点基因名
- SSR1
- 基因别名
- TRAPA
- UniProt
- P43307
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Signal sequence receptor subunit 1 (SSR1), also known as TRAP alpha, is a type I glycosylated membrane protein located in the endoplasmic reticulum (ER). It serves as the alpha subunit of the heterotetrameric translocon-associated protein (TRAP) complex, which is essential for the co-translational translocation of secretory and membrane proteins across the ER membrane. SSR1 functions as a membrane-bound chaperone that facilitates the proper folding of nascent polypeptides and contributes to calcium binding and the retention of ER-resident proteins. Its fundamental role in protein biogenesis is underscored by the fact that its loss leads to neonatal lethality and severe developmental defects. Clinically, dysregulated SSR1 expression has been linked to various malignancies, including diffuse large B-cell lymphoma and hypopharyngeal squamous cell carcinoma, where it may participate in oncogenic signaling axes.