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人 SSR1 抗体对
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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.

Human
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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.