| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HIST1H4I |
| Uniprot No | P62805 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-103aa |
| 氨基酸序列 | MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGPIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG |
| 分子量 | 37.07 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人HIST1H4I蛋白的模拟参考文献示例(注：文献及作者为虚构，仅供示例参考)：
1. **文献名称**：**《重组人HIST1H4I蛋白在大肠杆菌中的高效表达与纯化》**
**作者**：Zhang et al.
**摘要**：本文报道了利用大肠杆菌系统高效表达重组人HIST1H4I蛋白的优化方法，通过密码子优化和诱导条件调控提高蛋白产量，并采用镍柱亲和层析技术纯化获得高纯度蛋白，Western blot验证其特异性。
2. **文献名称**：**《HIST1H4I在染色质重塑中的相互作用网络分析》**
**作者**：Li & Wang
**摘要**：研究通过重组HIST1H4I蛋白进行体外Pull-down实验，发现其与组蛋白乙酰转移酶p300存在直接相互作用，暗示其在染色质结构调控和表观遗传修饰中的潜在功能。
3. **文献名称**：**《重组HIST1H4I通过调控细胞周期抑制肿瘤生长》**
**作者**：Chen et al.
**摘要**：利用重组HIST1H4I蛋白处理肝癌细胞，发现其通过上调p21表达阻滞细胞周期于G1期，并抑制肿瘤增殖，提示其作为癌症治疗靶点的潜力。
4. **文献名称**：**《HIST1H4I的赖氨酸乙酰化修饰对DNA修复的影响》**
**作者**：Kimura et al.
**摘要**：研究利用重组HIST1H4I蛋白结合质谱分析，鉴定其K8位点的乙酰化修饰，并证实该修饰增强了DNA损伤修复相关蛋白BRCA1的结合活性。
(注：以上文献为模拟内容，实际研究需通过学术数据库检索。)
The human HIST1H4I protein, a member of the histone H4 family, plays a critical role in chromatin structure and epigenetic regulation. Histones are essential for DNA packaging into nucleosomes, with H4 forming a tetrameric core alongside two H2A-H2B dimers and an H3-H4 heterodimer. The HIST1H4I gene, located within the HIST1 cluster on chromosome 6. encodes one of 11 H4 isoforms. While H4 proteins are highly conserved, subtle sequence variations in HIST1H4I may influence nucleosome stability and site-specific post-translational modifications like acetylation or methylation, which regulate gene expression and DNA repair.
Recombinant HIST1H4I is produced in heterologous systems (e.g., E. coli or mammalian cells) using genetic engineering techniques, enabling high-purity, standardized protein yields. This synthetic approach bypasses challenges in isolating natural histones while retaining biological activity. Recombinant forms are particularly valuable for studying chromatin dynamics, enzyme-substrate relationships in histone-modifying pathways, and mutations linked to diseases such as cancer, where aberrant H4 expression correlates with tumor progression. They also serve as critical tools for structural studies (e.g., X-ray crystallography) and drug discovery targeting epigenetic mechanisms. Recent interest focuses on its non-canonical roles in antimicrobial response and metabolic regulation, expanding its research scope beyond traditional epigenetics.
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