抗人 ASF1A 抗体对
01AB03361
Anti-silencing function 1A histone chaperone (ASF1A) is a highly conserved protein that serves as a primary chaperone for H3/H4 dimers, facilitating nucleosome assembly, disassembly, and exchange. It operates through both replication-dependent and replication-independent pathways by cooperating with chromatin assembly factor 1 (CAF-1) and HIRA, respectively. Structurally, ASF1A binds the H3/H4 heterodimer to prevent the formation of H3/H4 tetramers, a mechanism essential for DNA replication, transcription, and repair. The protein also promotes homologous recombination by recruiting MMS22L-TONSL and RAD51 to double-strand breaks. Furthermore, ASF1A interacts with importin-4 for the nuclear transport of newly synthesized histones and forms complexes with HAT1 and sNASP to ensure proper histone folding and deposition. These interactions are critical for maintaining genomic stability and epigenetic inheritance across diverse cellular processes.
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技术参数
- 靶点基因名
- ASF1A
- 蛋白别名
- anti-silencing function 1A histone chaperone; ASF1A
- UniProt
- Q9Y294
- 物种
- Human
产品详情
- 靶点名称
- ASF1A
- 蛋白名称
- anti-silencing function 1A histone chaperone
- 蛋白别名
- Histone chaperone ASF1A; Anti-silencing function protein 1 homolog A; hAsf1; hAsf1a; CCG1-interacting factor A; CIA; hCIA
- 靶点基因名
- ASF1A
- UniProt
- Q9Y294
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Anti-silencing function 1A histone chaperone (ASF1A) is a highly conserved protein that serves as a primary chaperone for H3/H4 dimers, facilitating nucleosome assembly, disassembly, and exchange. It operates through both replication-dependent and replication-independent pathways by cooperating with chromatin assembly factor 1 (CAF-1) and HIRA, respectively. Structurally, ASF1A binds the H3/H4 heterodimer to prevent the formation of H3/H4 tetramers, a mechanism essential for DNA replication, transcription, and repair. The protein also promotes homologous recombination by recruiting MMS22L-TONSL and RAD51 to double-strand breaks. Furthermore, ASF1A interacts with importin-4 for the nuclear transport of newly synthesized histones and forms complexes with HAT1 and sNASP to ensure proper histone folding and deposition. These interactions are critical for maintaining genomic stability and epigenetic inheritance across diverse cellular processes.