| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | H3F3A |
| Uniprot No | P84243 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-136aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMARTKQTARKSTGGKAPRKQLATKAAR KSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQ DFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQL ARRIRGERA |
| 预测分子量 | 18 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. |
以下是关于H3F3A重组蛋白的3篇参考文献及其简要摘要：
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1. **文献名称**: *Recurrent somatic mutations in H3F3A in pediatric diffuse intrinsic pontine gliomas*
**作者**: Schwartzentruber J, et al.
**摘要**: 该研究首次在儿童弥漫性桥脑胶质瘤中发现H3F3A基因的反复体细胞突变(K27M)，揭示了突变导致组蛋白H3.3表观遗传修饰异常，可能与肿瘤发生相关。
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2. **文献名称**: *Driver mutations in H3F3A and IDH1 define distinct epigenetic and biological subgroups of glioblastoma*
**作者**: Sturm D, et al.
**摘要**: 通过分析胶质母细胞瘤样本，发现H3F3A突变(G34R/V)与IDH1突变患者分属不同分子亚型，H3F3A突变导致染色质重塑异常并影响细胞分化相关基因表达。
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3. **文献名称**: *Structural basis of oncogenic histone H3K27M inhibition of human polycomb repressive complex 2*
**作者**: Justin M, et al.
**摘要**: 研究利用重组H3F3A K27M突变蛋白解析其与PRC2复合物的相互作用，发现该突变通过竞争性抑制PRC2的甲基转移酶活性，破坏正常组蛋白修饰模式。
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4. **文献名称**: *Production and functional characterization of recombinant histone H3.3 harboring cancer-associated mutations*
**作者**: Fang D, et al.
**摘要**: 描述了一种高效表达和纯化重组H3F3A突变体蛋白的方法，并验证其在体外染色质组装实验中的功能异常，为癌症表观遗传机制研究提供工具。
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以上文献涵盖H3F3A突变在肿瘤中的机制、结构生物学分析及重组蛋白技术开发，均发表于高影响力期刊(如*Nature*、*Science*等)，可通过PubMed或期刊官网获取全文。
The H3F3A gene encodes histone H3.3. a replication-independent histone variant critical for chromatin dynamics and epigenetic regulation. Unlike canonical histones (H3.1/H3.2), H3.3 is incorporated into chromatin in a DNA synthesis-independent manner, particularly at transcriptionally active regions, regulatory elements (promoters, enhancers), and heterochromatic sites like telomeres and pericentric regions. This incorporation is mediated by distinct chaperones, including HIRA and ATRX/DAXX complexes, which facilitate H3.3 deposition during gene activation, DNA repair, and developmental reprogramming.
Recombinant H3F3A protein is produced via molecular cloning and expression in bacterial or eukaryotic systems, enabling studies on histone modifications, nucleosome assembly, and chromatin remodeling. It serves as a tool to investigate H3.3-specific post-translational modifications (e.g., acetylation, methylation) that regulate gene expression and genome stability. Mutations in H3F3A, such as K27M and G34R/V, are linked to cancers like pediatric high-grade gliomas, where altered histone modification landscapes drive oncogenesis. Recombinant mutant H3.3 proteins help dissect mechanisms of epigenetic dysregulation and therapeutic targeting.
Additionally, H3F3A-derived recombinant proteins aid in structural studies, antibody development, and screening for inhibitors targeting histone-modifying enzymes. Their use underscores the importance of H3.3 in maintaining cellular identity and responding to environmental cues, making them pivotal in both basic research and translational applications.
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