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人 GRASP65 抗体对
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人 GRASP65 抗体对

01AB00510

Golgi reassembly-stacking protein 1 (GORASP1), also known as GRASP65, is a crucial peripheral membrane protein encoded by the GORASP1 gene in humans. It plays a significant role in maintaining the structure of the Golgi apparatus by facilitating the stacking of Golgi cisternae and linking them into larger ribbons through its interactions with other proteins, such as GM130 and p115. GORASP1 is essential for the proper functioning of the Golgi complex, particularly in protein sorting and modification processes. Additionally, it is implicated in apoptosis, as it serves as a substrate for caspase-3, leading to Golgi fragmentation during cell death. Dysregulation or mutations in GORASP1 have been associated with various diseases, including congenital disorders of glycosylation and immunodeficiencies.

Human
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技术参数

靶点基因名
GORASP1
基因别名
GOLPH5; GRASP65
蛋白别名
golgi reassembly stacking protein 1; GRASP65
UniProt
Q9BQQ3
物种
Human

产品详情

靶点名称
GRASP65
蛋白名称
golgi reassembly stacking protein 1
蛋白别名
Golgi reassembly-stacking protein 1; Golgi peripheral membrane protein p65; Golgi phosphoprotein 5; GOLPH5; Golgi reassembly-stacking protein of 65 kDa; GRASP65
靶点基因名
GORASP1
基因别名
GOLPH5; GRASP65
UniProt
Q9BQQ3
来源物种
Homo sapiens (Human)
物种反应性
Human

背景介绍

Golgi reassembly-stacking protein 1 (GORASP1), also known as GRASP65, is a crucial peripheral membrane protein encoded by the GORASP1 gene in humans. It plays a significant role in maintaining the structure of the Golgi apparatus by facilitating the stacking of Golgi cisternae and linking them into larger ribbons through its interactions with other proteins, such as GM130 and p115. GORASP1 is essential for the proper functioning of the Golgi complex, particularly in protein sorting and modification processes. Additionally, it is implicated in apoptosis, as it serves as a substrate for caspase-3, leading to Golgi fragmentation during cell death. Dysregulation or mutations in GORASP1 have been associated with various diseases, including congenital disorders of glycosylation and immunodeficiencies.