
人 BORCS6 抗体对
01AB01441
BLOC-1 related complex subunit 6 (BORCS6) is a protein component of the BORC complex, which is crucial for the movement and peripheral localization of lysosomes within cells. BORCS6 enables identical protein binding activity and is directly involved in lysosome positioning, as well as in the fusion of endosomes and autophagosomes, processes essential for efficient endo-lysosomal degradation. Structurally, BORCS6 is also known as C17orf59 and interacts with other BORC complex subunits to regulate lysosomal trafficking and cellular homeostasis. Disruption of BORCS6 function impairs lysosomal positioning and fusion, leading to developmental abnormalities, such as increased late endosomes, abnormal nuclei, and delayed embryonic development, particularly affecting gastrulation and the balance of embryonic cell lineages.
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技术参数
- 靶点基因名
- BORCS6
- 基因别名
- C17orf59
- 蛋白别名
- BLOC-1 related complex subunit 6; BORCS6
- UniProt
- Q96GS4
- 物种
- Human
产品详情
- 靶点名称
- BORCS6
- 蛋白名称
- BLOC-1 related complex subunit 6
- 蛋白别名
- BLOC-1-related complex subunit 6; Lysosome-dispersing protein; Lyspersin
- 靶点基因名
- BORCS6
- 基因别名
- C17orf59
- UniProt
- Q96GS4
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
BLOC-1 related complex subunit 6 (BORCS6) is a protein component of the BORC complex, which is crucial for the movement and peripheral localization of lysosomes within cells. BORCS6 enables identical protein binding activity and is directly involved in lysosome positioning, as well as in the fusion of endosomes and autophagosomes, processes essential for efficient endo-lysosomal degradation. Structurally, BORCS6 is also known as C17orf59 and interacts with other BORC complex subunits to regulate lysosomal trafficking and cellular homeostasis. Disruption of BORCS6 function impairs lysosomal positioning and fusion, leading to developmental abnormalities, such as increased late endosomes, abnormal nuclei, and delayed embryonic development, particularly affecting gastrulation and the balance of embryonic cell lineages.