人 TDP-25/TDP-35/TDP-43 抗体对
01AB04188
TDP-43 (TAR DNA-binding protein 43) is a critical RNA-binding protein that plays a vital role in RNA metabolism, including splicing and transport. It is primarily localized in the nucleus but mislocalizes to the cytoplasm in various neurodegenerative diseases, leading to the formation of pathological aggregates. Two notable fragments of TDP-43 are TDP-25 and TDP-35, which arise from caspase cleavage and are implicated in the pathogenesis of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). TDP-43 proteinopathy is characterized by hyperphosphorylated and ubiquitinated inclusions, with up to 97% of sporadic ALS cases exhibiting these aggregates. The accumulation of TDP-25 and TDP-35 disrupts normal cellular functions, contributing to neurotoxicity and neuronal death. Mutations in the TARDBP gene enhance the aggregation propensity of TDP-43 and its fragments, exacerbating their toxic effects.
| 规格 | 起售价 |
|---|---|
| 登录后可查看 | |
技术参数
- 靶点基因名
- TARDBP
- 基因别名
- TDP43
- 蛋白别名
- TAR DNA binding protein; TDP-25 / TDP-35 / TDP-43
- UniProt
- Q13148
- 物种
- Human
产品详情
- 靶点名称
- TDP-25 / TDP-35 / TDP-43
- 蛋白名称
- TAR DNA binding protein
- 蛋白别名
- TAR DNA-binding protein 43; TDP-43
- 靶点基因名
- TARDBP
- 基因别名
- TDP43
- UniProt
- Q13148
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
TDP-43 (TAR DNA-binding protein 43) is a critical RNA-binding protein that plays a vital role in RNA metabolism, including splicing and transport. It is primarily localized in the nucleus but mislocalizes to the cytoplasm in various neurodegenerative diseases, leading to the formation of pathological aggregates. Two notable fragments of TDP-43 are TDP-25 and TDP-35, which arise from caspase cleavage and are implicated in the pathogenesis of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). TDP-43 proteinopathy is characterized by hyperphosphorylated and ubiquitinated inclusions, with up to 97% of sporadic ALS cases exhibiting these aggregates. The accumulation of TDP-25 and TDP-35 disrupts normal cellular functions, contributing to neurotoxicity and neuronal death. Mutations in the TARDBP gene enhance the aggregation propensity of TDP-43 and its fragments, exacerbating their toxic effects.