人 Hsp27 抗体对
01AB04056
Heat shock protein family B (small) member 1 (HSPB1), also known as HSP27, is a molecular chaperone that plays a critical role in cellular stress responses, particularly under thermal, oxidative, and proteotoxic stress. This 23 kDa protein is ubiquitously expressed and functions by preventing protein aggregation, aiding in the refolding of misfolded proteins, and maintaining cytoskeletal integrity. HSPB1 forms large oligomeric complexes that are essential for its chaperone activity. Mutations in the HSPB1 gene have been linked to various diseases, most notably Charcot-Marie-Tooth disease, a hereditary neuropathy characterized by muscle weakness and atrophy due to peripheral nerve degeneration. These mutations can disrupt normal oligomerization and protein interactions, leading to neurodegeneration and impaired cellular functions.
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技术参数
- 靶点基因名
- HSPB1
- 基因别名
- HSP27; HSP28
- 蛋白别名
- heat shock protein family B (small) member 1; Hsp27
- UniProt
- P04792
- 物种
- Human
产品详情
- 靶点名称
- Hsp27
- 蛋白名称
- heat shock protein family B (small) member 1
- 蛋白别名
- Heat shock protein beta-1; HspB1; 28 kDa heat shock protein; Estrogen-regulated 24 kDa protein; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27
- 靶点基因名
- HSPB1
- 基因别名
- HSP27; HSP28
- UniProt
- P04792
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Heat shock protein family B (small) member 1 (HSPB1), also known as HSP27, is a molecular chaperone that plays a critical role in cellular stress responses, particularly under thermal, oxidative, and proteotoxic stress. This 23 kDa protein is ubiquitously expressed and functions by preventing protein aggregation, aiding in the refolding of misfolded proteins, and maintaining cytoskeletal integrity. HSPB1 forms large oligomeric complexes that are essential for its chaperone activity. Mutations in the HSPB1 gene have been linked to various diseases, most notably Charcot-Marie-Tooth disease, a hereditary neuropathy characterized by muscle weakness and atrophy due to peripheral nerve degeneration. These mutations can disrupt normal oligomerization and protein interactions, leading to neurodegeneration and impaired cellular functions.