| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DDX27 |
| Uniprot No | Q96GQ7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-794aa |
| 氨基酸序列 | DNMLADLGLIGTIGEDDEVPVEPESDSGDEEEEGPIVLGRRQKALGKNRSADFNPDFVFTEKEGTYDGSWALADVMSQLKKKRAATTLDEKIEKVRKKRKTEDKEAKSGKLEKEKEAKEGSEPKEQEDLQENDEEGSEDEASETDYSSADENILTKADTLKVKDRKKKKKKGQEAGGFFEDASQYDENLSFQDMNLSRPLLKAITAMGFKQPTPIQKACIPVGLLGKDICACAATGTGKTAAFALPVLERLIYKPRQAPVTRVLVLVPTRELGIQVHSVTRQLAQFCNITTCLAVGGLDVKSQEAALRAAPDILIATPGRLIDHLHNCPSFHLSSIEVLILDEADRMLDEYFEEQMKEIIRMCSHHRQTMLFSATMTDEVKDLASVSLKNPVRIFVNSNTDVAPFLRQEFIRIRPNREGDREAIVAALLTRTFTDHVMLFTQTKKQAHRMHILLGLMGLQVGELHGNLSQTQRLEALRRFKDEQIDILVATDVAARGLDIEGVKTVINFTMPNTIKHYVHRVGRTARAGRAGRSVSLVGEDERKMLKEIVKAAKAPVKARILPQDVILKFRDKIEKMEKDVYAVLQLEAEEKEMQQSEAQINTAKRLLEKGKEAVVQEPERSWFQTKEERKKEKIAKALQEFDLALRGKKKRKKFMKDAKKKGEMTAEERSQFEILKAQMFAERLAKRNRRAKRARAMPEEEPVRGPAKKQKQGKKSVFDEELTNTSKKALKQYRAGPSFEERKQLGLPHQRRGGNFKSKSRYKR |
| 预测分子量 | 102.5 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. |
以下是关于DDX27重组蛋白的参考文献示例(注：以下内容为模拟生成，仅供参考)：
1. **文献名称**: "Structural and Biochemical Characterization of Recombinant Human DDX27 Reveals RNA Unwinding Activity"
**作者**: Müller, C.W., et al.
**摘要**: 本研究通过在大肠杆菌中表达并纯化重组人DDX27蛋白，揭示了其ATP依赖的RNA解旋酶活性。结构分析表明DDX27的DEAD-box结构域对RNA结合和ATP水解至关重要，并发现其参与核糖体RNA前体(pre-rRNA)的加工过程。
2. **文献名称**: "DDX27 Regulates Ribosome Biogenesis through Interaction with R-Loop Structures: Insights from Recombinant Protein Assays"
**作者**: Lee, S., et al.
**摘要**: 利用重组DDX27蛋白进行体外实验，发现其能够特异性结合R-loop结构并通过ATP酶活性重塑RNA-DNA杂交体，从而促进rRNA的成熟。研究强调了DDX27在核糖体生物合成中的调控作用。
3. **文献名称**: "Functional Analysis of Recombinant DDX27 in Viral RNA Replication and Host Interaction"
**作者**: Zhang, X., et al.
**摘要**: 该研究通过表达重组DDX27蛋白，证明其与多种病毒RNA直接结合，并增强病毒基因组的复制效率。实验表明DDX27的缺失显著抑制病毒增殖，提示其在宿主-病原体相互作用中的关键角色。
4. **文献名称**: "Mechanistic Insights into the ATPase Cycle of DDX27 Using Recombinant Protein and Single-Molecule Imaging"
**作者**: Johnson, R.K., et al.
**摘要**: 通过重组DDX27蛋白的单分子荧光实验，揭示了其ATP结合和水解的动态过程，并证明该蛋白通过构象变化促进RNA二级结构的解旋，为DDX27的分子机制提供了直接证据。
**备注**：上述文献为示例性内容，实际引用时请通过学术数据库(如PubMed、Web of Science)检索真实文献。
DDX27. a member of the DEAD-box RNA helicase family, plays critical roles in RNA metabolism and ribosome biogenesis. Characterized by its conserved Asp-Glu-Ala-Asp (DEAD) motif, this ATP-dependent enzyme facilitates RNA unwinding, structural remodeling, and protein-RNA interactions. It is predominantly localized in the nucleolus, where it participates in ribosomal RNA (rRNA) processing, a fundamental process for ribosome assembly and cellular protein synthesis. Studies suggest DDX27 also influences cell cycle progression, stress responses, and viral RNA surveillance, underscoring its multifaceted regulatory functions.
Recombinant DDX27 protein is engineered for in vitro studies to dissect its molecular mechanisms. Typically produced in Escherichia coli or mammalian expression systems, the protein retains enzymatic activity for functional assays, including ATPase and RNA helicase activity analyses. Its purification often involves affinity tags (e.g., His-tag) followed by chromatographic techniques. Researchers utilize recombinant DDX27 to investigate its interactions with RNA substrates, cofactors (e.g., non-structural viral proteins), or small-molecule inhibitors. Structural studies using recombinant protein have revealed domain-specific roles, such as the DEAD domain’s ATP-binding capacity and C-terminal regions mediating RNA recognition.
Dysregulation of DDX27 is linked to diseases, particularly cancers. Overexpression in colorectal and hepatocellular carcinomas correlates with poor prognosis, suggesting oncogenic potential. Conversely, reduced levels impair ribosome maturation, leading to cellular stress. Recombinant DDX37 serves as a tool for drug screening and mechanistic studies targeting RNA helicase-driven pathologies. Ongoing research aims to clarify its role in rRNA quality control pathways and therapeutic targeting opportunities.
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