| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | caf1 |
| Uniprot No | Q9UFF9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-292aa |
| 氨基酸序列 | MPAALVENSQVICEVWASNLEEEMRKIREIVLSYSYIAMDTEFPGVVVRPIGEFRSSIDYQYQLLRCNVDLLKIIQLGLTFTNEKGEYPSGINTWQFNFKFNLTEDMYSQDSIDLLANSGLQFQKHEEEGIDTLHFAELLMTSGVVLCDNVKWLSFHSGYDFGYMVKLLTDSRLPEEEHEFFHILNLFFPSIYDVKYLMKSCKNLKGGLQEVADQLDLQRIGRQHQAGSDSLLTGMAFFRMKELFFEDSIDDAKYCGRLYGLGTGVAQKQNEDVDSAQEKMSILAIINNMQQ |
| 预测分子量 | 60.5 kDa |
| 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3篇关于Caf1重组蛋白的典型参考文献(内容为模拟概括)：
1. **文献名称**: "High-level expression and purification of recombinant Caf1 protein from Yersinia pestis in Escherichia coli"
**作者**: Smith A, et al.
**摘要**: 研究利用大肠杆菌表达系统高效表达Caf1重组蛋白，通过优化启动子和培养条件获得高产量，并采用亲和层析纯化得到高纯度蛋白，为疫苗开发奠定基础。
2. **文献名称**: "Structural characterization of Caf1 polymer as a vaccine candidate against plague"
**作者**: Zhang Y, et al.
**摘要**: 通过X射线晶体学和电镜解析Caf1重组蛋白的多聚体结构，揭示其形成纤维状聚合物的分子机制，证实其在小鼠模型中诱导强效免疫应答的潜力。
3. **文献名称**: "Development of a thermostable Caf1 subunit vaccine using recombinant protein technology"
**作者**: Ivanova T, et al.
**摘要**: 通过基因工程技术改造Caf1重组蛋白的热稳定性，证明其在高温下仍保持抗原性，动物实验显示该改良蛋白可提供长效免疫保护，适用于热带地区疫苗存储。
(注：以上为基于领域知识的模拟文献，实际引用请以真实论文为准。)
**Background of CAF1 Recombinant Protein**
Chromatin Assembly Factor 1 (CAF1) is a conserved histone chaperone complex critical for DNA replication-coupled nucleosome assembly. It facilitates the deposition of histone H3/H4 tetramers onto newly synthesized DNA, ensuring proper chromatin structure and epigenetic inheritance. The CAF1 complex typically consists of three subunits (p150. p60. and p48 in humans), though recombinant forms often focus on the p150/p60 heterodimer, which retains core chaperone activity.
Recombinant CAF1 proteins are engineered using expression systems like *E. coli* or insect cells, enabling large-scale production for biochemical and structural studies. These proteins are indispensable for *in vitro* studies on chromatin dynamics, DNA repair, and replication. By providing a controlled source of CAF1. researchers can dissect its interactions with histones, DNA, and other chaperones (e.g., ASF1), as well as its role in maintaining genome stability.
Interest in CAF1 spans multiple fields. In epigenetics, it helps unravel mechanisms of histone recycling and modification propagation. In cancer biology, dysregulation of CAF1 is linked to replication stress and oncogenesis, making it a potential therapeutic target. Additionally, recombinant CAF1 supports synthetic biology efforts to reconstitute chromatin in minimal systems, advancing studies on gene regulation and nuclear organization.
The development of CAF1 recombinant tools has also addressed challenges in studying native complexes, which are low-abundance and difficult to purify. Engineered variants with tags (e.g., His-tags) simplify purification, while mutagenesis allows functional domain mapping. Overall, CAF1 recombinant proteins serve as a cornerstone for understanding chromatin biology and its implications in health and disease.
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