
人 TDP-35/TDP-43 抗体对
01AB04192
TDP-35 and TDP-43 are crucial proteins involved in RNA metabolism, with TDP-43 being a 43 kDa RNA-binding protein that plays a significant role in pre-mRNA processing. TDP-35, a C-terminal fragment of TDP-43, is generated through caspase cleavage and is implicated in neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). In these conditions, TDP-43 mislocalizes from the nucleus to the cytoplasm, forming aggregates that disrupt cellular function. TDP-35 can sequester full-length TDP-43 into cytoplasmic inclusions, leading to further dysfunction in RNA processing and contributing to neurodegeneration. Mutations in the TARDBP gene, which encodes TDP-43, have been linked to enhanced aggregation of these fragments, exacerbating their toxic effects. The relationship between TDP-35 and TDP-43 highlights the importance of these proteins in the pathogenesis of ALS and FTLD, where their aggregation leads to cellular stress and neuronal death.
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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-35 / TDP-43
- UniProt
- Q13148
- 物种
- Human
产品详情
- 靶点名称
- 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-35 and TDP-43 are crucial proteins involved in RNA metabolism, with TDP-43 being a 43 kDa RNA-binding protein that plays a significant role in pre-mRNA processing. TDP-35, a C-terminal fragment of TDP-43, is generated through caspase cleavage and is implicated in neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). In these conditions, TDP-43 mislocalizes from the nucleus to the cytoplasm, forming aggregates that disrupt cellular function. TDP-35 can sequester full-length TDP-43 into cytoplasmic inclusions, leading to further dysfunction in RNA processing and contributing to neurodegeneration. Mutations in the TARDBP gene, which encodes TDP-43, have been linked to enhanced aggregation of these fragments, exacerbating their toxic effects. The relationship between TDP-35 and TDP-43 highlights the importance of these proteins in the pathogenesis of ALS and FTLD, where their aggregation leads to cellular stress and neuronal death.