人 UBXN6 抗体对
01AB03426
UBX domain protein 6 (UBXN6) is a cytosolic protein that serves as a key cofactor for the AAA+ ATPase VCP/p97, negatively regulating its ATPase activity to coordinate various cellular degradation pathways. It is essential for endoplasmic reticulum-associated degradation of misfolded proteins, macroautophagy, and the clearance of damaged lysosomes. UBXN6 also facilitates the endosome-to-lysosome transport of caveolin-1 for degradation. In the context of the immune response, it has been shown to activate autophagy in macrophages and suppress inflammation via FOXO3 signaling, thereby mitigating mitochondrial stress. Clinically, UBXN6 is associated with inclusion body myopathy with early-onset Paget disease of bone and frontotemporal dementia, a multisystem degenerative disorder. Its role in maintaining lysosomal biogenesis and regulating immunometabolic shifts toward glycolysis further underscores its importance in both protein quality control and the systemic inflammatory response, particularly during conditions such as sepsis.
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技术参数
- 靶点基因名
- UBXN6
- 基因别名
- UBXD1; UBXDC2
- 蛋白别名
- UBX domain protein 6; UBXN6
- UniProt
- Q9BZV1
- 物种
- Human
产品详情
- 靶点名称
- UBXN6
- 蛋白名称
- UBX domain protein 6
- 蛋白别名
- UBX domain-containing protein 6; UBX domain-containing protein 1
- 靶点基因名
- UBXN6
- 基因别名
- UBXD1; UBXDC2
- UniProt
- Q9BZV1
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
UBX domain protein 6 (UBXN6) is a cytosolic protein that serves as a key cofactor for the AAA+ ATPase VCP/p97, negatively regulating its ATPase activity to coordinate various cellular degradation pathways. It is essential for endoplasmic reticulum-associated degradation of misfolded proteins, macroautophagy, and the clearance of damaged lysosomes. UBXN6 also facilitates the endosome-to-lysosome transport of caveolin-1 for degradation. In the context of the immune response, it has been shown to activate autophagy in macrophages and suppress inflammation via FOXO3 signaling, thereby mitigating mitochondrial stress. Clinically, UBXN6 is associated with inclusion body myopathy with early-onset Paget disease of bone and frontotemporal dementia, a multisystem degenerative disorder. Its role in maintaining lysosomal biogenesis and regulating immunometabolic shifts toward glycolysis further underscores its importance in both protein quality control and the systemic inflammatory response, particularly during conditions such as sepsis.