人 TDP-43 抗体对
01AB04194
TDP-43 (TAR DNA-binding protein 43) is a nuclear RNA/DNA-binding protein involved in RNA metabolism, including splicing and transport. Its pathological forms, TDP-25 and TDP-35, are C-terminal fragments generated through caspase cleavage, which contribute to neurodegenerative diseases like amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). TDP-43 mislocalizes from the nucleus to the cytoplasm, forming aggregates that disrupt normal cellular functions; this phenomenon is observed in approximately 97% of sporadic ALS cases and about 45% of FTLD cases. The accumulation of hyperphosphorylated and ubiquitinated TDP-43 inclusions leads to neurotoxicity through mechanisms such as loss of nuclear function and gain of toxic properties in the cytoplasm. Mutations in the TARDBP gene, particularly in the C-terminal domain, enhance the aggregation propensity of TDP-43, exacerbating its role in disease progression.
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技术参数
- 靶点基因名
- TARDBP
- 基因别名
- TDP43
- 蛋白别名
- TAR DNA binding protein; TDP-43
- UniProt
- Q13148
- 物种
- Human
产品详情
- 靶点名称
- 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 nuclear RNA/DNA-binding protein involved in RNA metabolism, including splicing and transport. Its pathological forms, TDP-25 and TDP-35, are C-terminal fragments generated through caspase cleavage, which contribute to neurodegenerative diseases like amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). TDP-43 mislocalizes from the nucleus to the cytoplasm, forming aggregates that disrupt normal cellular functions; this phenomenon is observed in approximately 97% of sporadic ALS cases and about 45% of FTLD cases. The accumulation of hyperphosphorylated and ubiquitinated TDP-43 inclusions leads to neurotoxicity through mechanisms such as loss of nuclear function and gain of toxic properties in the cytoplasm. Mutations in the TARDBP gene, particularly in the C-terminal domain, enhance the aggregation propensity of TDP-43, exacerbating its role in disease progression.