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人 TDP-35/TDP-43 抗体对
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人 TDP-35/TDP-43 抗体对

01AB04191

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.

Human
规格起售价
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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.