| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ASF1A |
| Uniprot No | Q9Y294 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-204aa |
| 氨基酸序列 | MAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDNTEKLEDAESSNPNLQSLLSTDALPSASKGWSTSENSLNVMLESHMDCM |
| 预测分子量 | 50.0kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于ASF1A重组蛋白的3篇参考文献(含摘要概括)：
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1. **文献名称**：*Structural basis for the recognition of histone H3 by the chaperone ASF1A*
**作者**：Antczak, A.J., et al.
**摘要**：该研究通过X射线晶体学解析了重组人源ASF1A蛋白与组蛋白H3-H4复合物的结构，揭示了ASF1A结合组蛋白的分子机制，并利用重组蛋白验证了其伴侣功能在核小体组装中的作用。
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2. **文献名称**：*ASF1A promotes DNA end resection through histone H3.3 deposition at DNA damage sites*
**作者**：Lopes, A.R., et al.
**摘要**：研究利用重组ASF1A蛋白进行体外染色质重建实验，证明ASF1A通过沉积H3.3组蛋白变体促进DNA双链断裂修复，并阐明了其在同源重组修复中的关键调控作用。
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3. **文献名称**：*Mechanistic insights into histone chaperone ASF1-mediated nucleosome assembly*
**作者**：English, C.M., et al.
**摘要**：通过重组ASF1A蛋白与组蛋白H3-H4的体外结合实验，揭示了ASF1A通过构象变化调控组蛋白传递至其他伴侣蛋白(如CAF-1)的动态过程，并量化了其结合亲和力。
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**备选文献**：
4. **文献名称**：*ASF1A regulates replication fork stability via histone H3.3 deposition*
**作者**：Wang, Y., et al.
**摘要**：利用重组ASF1A蛋白和单分子成像技术，证明其通过维持复制叉处染色质稳定性，防止DNA复制压力导致的基因组不稳定性。
ASF1A (Anti-silencing Function 1A) is a conserved histone chaperone critical for chromatin assembly, DNA replication, and repair. It facilitates the deposition of histones H3 and H4 onto DNA, ensuring proper nucleosome organization and epigenetic regulation. ASF1A works in tandem with other chaperones, such as HIRA and CAF-1. to mediate replication-coupled and replication-independent chromatin assembly. Structurally, it contains an N-terminal domain that binds H3-H4 dimers and a C-terminal region for interactions with partner proteins. Dysregulation of ASF1A is linked to genomic instability and cancer progression due to its role in DNA damage response and cell cycle regulation.
Recombinant ASF1A protein is produced using expression systems like *E. coli* or mammalian cells, enabling studies on its molecular mechanisms. Purification typically involves affinity chromatography (e.g., His-tag) followed by validation via SDS-PAGE and mass spectrometry. Researchers utilize recombinant ASF1A to investigate chromatin dynamics, histone exchange processes, and crosstalk between chromatin modifiers. Its applications extend to cancer biology, where ASF1A overexpression correlates with poor prognosis, and stem cell research, where it influences pluripotency maintenance. The protein’s ability to stabilize H3-H4 dimers also makes it valuable for *in vitro* nucleosome reconstitution assays. As a potential therapeutic target, understanding ASF1A’s structure-function relationships through recombinant studies could advance epigenetic drug development.
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