人 ATXN2 抗体对
01AB03561
Ataxin 2 (ATXN2) is a multifunctional, evolutionarily conserved cytoplasmic RNA-binding protein that localizes to the endoplasmic reticulum and plasma membrane. It plays a central role in post-transcriptional regulation, including mRNA stabilization, translation via polyribosome assembly, and the formation of stress granules and P-bodies. These functions are mediated through its two LSm domains and a PAM2 motif, the latter of which facilitates interaction with poly(A)-binding protein. ATXN2 also influences endocytic trafficking, cytoskeletal dynamics, and mitochondrial function. Clinically, pathogenic expansions of its N-terminal polyglutamine tract are the established cause of spinocerebellar ataxia type 2, a neurodegenerative disorder characterized by cerebellar atrophy and motor deficits. Furthermore, intermediate polyglutamine expansions are recognized as significant risk factors for amyotrophic lateral sclerosis and frontotemporal dementia, where they promote the toxic aggregation of proteins such as TDP-43 and FUS.
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技术参数
- 靶点基因名
- ATXN2
- 基因别名
- ATX2; SCA2; TNRC13
- 蛋白别名
- ataxin 2; ATXN2
- UniProt
- Q99700
- 物种
- Human
产品详情
- 靶点名称
- ATXN2
- 蛋白名称
- ataxin 2
- 蛋白别名
- Ataxin-2; Spinocerebellar ataxia type 2 protein; Trinucleotide repeat-containing gene 13 protein
- 靶点基因名
- ATXN2
- 基因别名
- ATX2; SCA2; TNRC13
- UniProt
- Q99700
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Ataxin 2 (ATXN2) is a multifunctional, evolutionarily conserved cytoplasmic RNA-binding protein that localizes to the endoplasmic reticulum and plasma membrane. It plays a central role in post-transcriptional regulation, including mRNA stabilization, translation via polyribosome assembly, and the formation of stress granules and P-bodies. These functions are mediated through its two LSm domains and a PAM2 motif, the latter of which facilitates interaction with poly(A)-binding protein. ATXN2 also influences endocytic trafficking, cytoskeletal dynamics, and mitochondrial function. Clinically, pathogenic expansions of its N-terminal polyglutamine tract are the established cause of spinocerebellar ataxia type 2, a neurodegenerative disorder characterized by cerebellar atrophy and motor deficits. Furthermore, intermediate polyglutamine expansions are recognized as significant risk factors for amyotrophic lateral sclerosis and frontotemporal dementia, where they promote the toxic aggregation of proteins such as TDP-43 and FUS.