抗人 HSP90AA4P 抗体对
01AB01156
Heat shock protein 90 alpha family class A member 4 (HSP90AA4P), a putative molecular chaperone with a length of 418 amino acids, predicted to promote the maturation, structural maintenance, and proper regulation of target proteins. It likely displays ATP binding and hydrolysis activities, unfolded protein binding, and contributes to cellular processes such as response to heat, protein folding, and stabilization. Predicted cytoplasmic localization suggests involvement in protein-containing complexes within neuronal cells and the perinuclear cytoplasmic region. As a member of the Hsp90 family, it shares similarities with functional Hsp90 isoforms, which are critical ATP-dependent chaperones facilitating the folding and stabilization of numerous client proteins under both normal and stress conditions. Dysregulation of Hsp90 chaperones is linked to cancer, neurodegenerative diseases, and infection, reflecting the broad clinical relevance of this protein family.
| 规格 | 起售价 |
|---|---|
| 登录后可查看 | |
技术参数
- 靶点基因名
- HSP90AA4P
- 基因别名
- HSP90AD; HSPCAL2
- 蛋白别名
- heat shock protein 90 alpha family class A member 4, pseudogene; HSP90AA4P
- UniProt
- Q58FG1
- 物种
- Human
产品详情
- 靶点名称
- HSP90AA4P
- 蛋白名称
- heat shock protein 90 alpha family class A member 4, pseudogene
- 蛋白别名
- Putative heat shock protein HSP 90-alpha A4; Heat shock 90 kDa protein 1 alpha-like 2; Heat shock protein 90-alpha D; Heat shock protein 90Ad
- 靶点基因名
- HSP90AA4P
- 基因别名
- HSP90AD; HSPCAL2
- UniProt
- Q58FG1
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Heat shock protein 90 alpha family class A member 4 (HSP90AA4P), a putative molecular chaperone with a length of 418 amino acids, predicted to promote the maturation, structural maintenance, and proper regulation of target proteins. It likely displays ATP binding and hydrolysis activities, unfolded protein binding, and contributes to cellular processes such as response to heat, protein folding, and stabilization. Predicted cytoplasmic localization suggests involvement in protein-containing complexes within neuronal cells and the perinuclear cytoplasmic region. As a member of the Hsp90 family, it shares similarities with functional Hsp90 isoforms, which are critical ATP-dependent chaperones facilitating the folding and stabilization of numerous client proteins under both normal and stress conditions. Dysregulation of Hsp90 chaperones is linked to cancer, neurodegenerative diseases, and infection, reflecting the broad clinical relevance of this protein family.