人 POMP 抗体对
01AB02872
Proteasome maturation protein (POMP) is an essential chaperone that orchestrates the biogenesis of the 20S proteasome core complex, a central component of the cellular protein degradation machinery. POMP localizes to the endoplasmic reticulum (ER), where it binds to α1–7 rings of the assembling proteasome, recruits β-subunits in a stepwise manner, and mediates the association of precursor complexes with the ER membrane, thereby coordinating the assembly and maturation process to ensure efficient formation of functional proteasomes. The degradation of POMP itself is tightly regulated by a dual-checking mechanism, with the α5 subunit sensing POMP degradation to trigger the release of other assembly chaperones, thus safeguarding the fidelity of proteasome maturation. Defects in POMP function or expression can impair proteasome assembly, leading to reduced proteolytic capacity and contributing to diseases characterized by protein aggregation and impaired protein homeostasis, such as certain autoinflammatory syndromes and age-related disorders.
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技术参数
- 靶点基因名
- POMP
- 基因别名
- C13orf12; UMP1
- 蛋白别名
- proteasome maturation protein; POMP
- UniProt
- Q9Y244
- 物种
- Human
产品详情
- 靶点名称
- POMP
- 蛋白名称
- proteasome maturation protein
- 蛋白别名
- Proteasome maturation protein; Proteassemblin; Protein UMP1 homolog; hUMP1; Voltage-gated K channel beta subunit 4.1
- 靶点基因名
- POMP
- 基因别名
- C13orf12; UMP1
- UniProt
- Q9Y244
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Proteasome maturation protein (POMP) is an essential chaperone that orchestrates the biogenesis of the 20S proteasome core complex, a central component of the cellular protein degradation machinery. POMP localizes to the endoplasmic reticulum (ER), where it binds to α1–7 rings of the assembling proteasome, recruits β-subunits in a stepwise manner, and mediates the association of precursor complexes with the ER membrane, thereby coordinating the assembly and maturation process to ensure efficient formation of functional proteasomes. The degradation of POMP itself is tightly regulated by a dual-checking mechanism, with the α5 subunit sensing POMP degradation to trigger the release of other assembly chaperones, thus safeguarding the fidelity of proteasome maturation. Defects in POMP function or expression can impair proteasome assembly, leading to reduced proteolytic capacity and contributing to diseases characterized by protein aggregation and impaired protein homeostasis, such as certain autoinflammatory syndromes and age-related disorders.