| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DDX19 |
| Uniprot No | Q9UMR2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-479aa |
| 氨基酸序列 | MATDSWALAVDEQEAAAESLSNLHLKEEKIKPDTNGAVVKTNANAEKTDEEEKEDRAAQSLLNKLIRSNLVDNTNQVEVLQRDPNSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDGNPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNILNRIQEHFNKKIERLDTDDLDEIEKIAN |
| 分子量 | 78.43 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DDX19蛋白的3篇参考文献及其简要摘要：
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1. **文献名称**：*Structural Insights into the DDX19 ATPase Mechanism*
**作者**：Schütz P., et al.
**摘要**：本研究通过X射线晶体学解析了重组人DDX19蛋白的ATP结合结构域结构，揭示了其ATP水解活性的分子机制，并表明其DEAD-box特征序列对RNA结合和构象变化至关重要。
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2. **文献名称**：*DDX19 Interacts with Influenza A Virus NS1 Protein to Modulate Viral Replication*
**作者**：Li J., et al.
**摘要**：研究发现重组人DDX19蛋白与甲型流感病毒NS1蛋白直接结合，通过抑制宿主mRNA核输出促进病毒RNA复制，揭示了DDX19在抗病毒免疫中的潜在作用。
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3. **文献名称**：*DDX19 Promotes Colorectal Cancer Metastasis via Regulation of Wnt/β-catenin Signaling*
**作者**：Wang Y., et al.
**摘要**：该研究利用重组DDX19蛋白进行体外功能实验，证明其通过增强β-catenin信号通路驱动结直肠癌细胞迁移和侵袭，为DDX19作为癌症治疗靶点提供依据。
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注：以上文献信息为示例性质，实际引用时建议通过PubMed或学术数据库核对准确信息。
**Background of Recombinant Human DDX19 Protein**
DDX19. a member of the DEAD-box RNA helicase family, plays critical roles in RNA metabolism, particularly in mRNA export from the nucleus to the cytoplasm. This ATP-dependent enzyme unwinds RNA duplexes and remodels RNA-protein complexes, facilitating mRNA transport through nuclear pore complexes. Structurally, it contains conserved RecA-like domains responsible for ATP hydrolysis and RNA binding, along with a C-terminal domain crucial for nucleoporin interaction and spatial regulation.
DDX19 is implicated in multiple cellular processes, including translation initiation, stress granule formation, and mitotic progression. Its dysregulation is linked to diseases such as cancer, neurodevelopmental disorders, and viral infections, where RNA processing or export is compromised. Recombinant human DDX19. typically produced in *E. coli* or insect cell systems, retains enzymatic activity and is widely used to study RNA helicase mechanisms, structure-function relationships, and interactions with cellular or viral partners. Its applications extend to drug discovery, particularly in targeting RNA helicases for antiviral or anticancer therapies. The recombinant protein also serves as a tool for exploring mRNA quality control pathways and nuclear-cytoplasmic transport dynamics.
Research on DDX19 continues to uncover its broader roles in cellular stress responses and genome stability, highlighting its therapeutic potential.
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