| 纯度 | >80%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PHF5A |
| Uniprot No | Q7RTV0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-110aa |
| 氨基酸序列 | MAKHHPDLIFCRKQAGVAIGRLCEKCDGKCVICDSYVRPCTLVRICDECNYGSYQGRCVICGGPGVSDAYYCKECTIQEKDRDGCPKIVNLGSSKTDLFYERKKYGFKKR |
| 预测分子量 | 39.4kDa |
| 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PHF5A重组蛋白的3篇参考文献及其简要摘要：
1. **文献名称**：*PHF5A promotes spliceosome remodeling and its mutation is linked to myelodysplastic syndromes*
**作者**：Tang Q, et al.
**摘要**：该研究利用重组PHF5A蛋白，揭示了其在剪接体重塑中的关键作用，并通过突变分析发现PHF5A突变与骨髓增生异常综合征(MDS)的发生相关，表明其异常表达可能影响RNA剪接的保真性。
2. **文献名称**：*Structural basis of PHF5A recognition by the spliceosome assembly factor SART3*
**作者**：Zhang Y, et al.
**摘要**：通过重组PHF5A蛋白的晶体结构解析，阐明了其与剪接体组装因子SART3的相互作用机制，揭示了PHF5A在剪接体早期组装中的结构基础。
3. **文献名称**：*PHF5A regulates cellular proliferation and chemoresistance in triple-negative breast cancer via c-Myc signaling*
**作者**：Wang L, et al.
**摘要**：研究利用重组PHF5A蛋白进行功能实验，发现其通过调控c-Myc信号通路影响三阴性乳腺癌细胞的增殖和化疗耐药性，为靶向PHF5A的癌症治疗提供了依据。
以上文献均涉及重组PHF5A蛋白在剪接体功能或癌症机制研究中的应用。如需具体期刊或年份信息可进一步补充。
PHF5A (PHD Finger Protein 5A) is a conserved eukaryotic protein belonging to the PHD finger protein family, characterized by its plant homeodomain (PHD) zinc finger motif. It plays critical roles in transcriptional regulation, pre-mRNA splicing, and chromatin remodeling. PHF5A interacts with the spliceosome component SF3b, a subcomplex of the U2 small nuclear ribonucleoprotein (snRNP), and is essential for maintaining spliceosome stability and catalytic activity. Studies suggest its involvement in recognizing specific intronic branchpoint sequences, ensuring accurate splicing. Dysregulation of PHF5A has been linked to cancers, neurodegenerative diseases, and developmental disorders, highlighting its biological significance.
Recombinant PHF5A protein is engineered using expression systems like *E. coli* or mammalian cells to produce purified, functional PHF5A for research. Its recombinant form enables structural studies, such as crystallography or cryo-EM, to map interaction interfaces with spliceosomal components. Additionally, it facilitates biochemical assays to dissect PHF5A’s role in splicing regulation and its partnership with proteins like SF3B1. Researchers also use it to screen for inhibitors targeting PHF5A in cancer therapy, as its overexpression in tumors correlates with poor prognosis. The protein’s PHD domain, critical for chromatin interactions, is a focus in epigenetic studies. Recombinant PHF5A thus serves as a vital tool for unraveling molecular mechanisms in gene expression and disease pathogenesis.
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