| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DHX33 |
| Uniprot No | Q9H6R0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-707aa |
| 氨基酸序列 | MPEEAGFPPAKRFRPGSGPPSRAGSFPPGRQVVMLLTAGSGGRGGGGGRRQQPPLAQPSASPYPEAVELQRRSLPIFQARGQLLAQLRNLDNAVLIGETGSGKTTQIPQYLYEGGISRQGIIAVTQPRRVAAISLATRVSDEKRTELGKLVGYTVRFDDVTSEDTRIKFLTDGMLLREAISDSLLRKYSCVILDEAHERTIHTDVLFGVVKAAQKRRKELGKLPLKVIVMSATMDVDLFSQYFNGAPVLYLEGRQHPIQVFYTKQPQNDYLHAALVSVFQIHQEAPSSQDILVFLTGQEEIEAMSKTCRDIAKHLPDGCPAMLVLPLYASLPYAQQLRVFQGAPKGYRKVIISTNIAETSITITGIKYVVDTGMVKAKKYNPDSGLEVLAVQRVSKTQAWQRTGRAGREDSGICYRLYTEDEFEKFDKMTVPEIQRCNLASVMLQLLAMKVPNVLTFDFMSKPSPDHIQAAIAQLDLLGALEHKDDQLTLTPMGRKMAAFPLEPKFAKTILMSPKFHCTEEILTIVSLLSVDSVLHNPPSRREEVQGVRKKFISSEGDHMTLLNIYRTFKNLGGNKDWCKENFVNSKNMTLVAEVRAQLRDICLKMSMPIASSRGDVESVRRCLAHSLFMSTAELQPDGTYATTDTHQPVAIHPSSVLFHCKPACVVYTELLYTNKCYMRDLCVIDAQWLYEAAPEYFRRKLRTARN |
| 预测分子量 | 78,8 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DHX33重组蛋白的3篇参考文献，按研究方向和摘要内容概括整理：
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1. **文献名称**：*DHX33 interacts with AP-1 to regulate c-MYC transcription in colorectal cancer*
**作者**：Zhang Y, et al.
**摘要**：该研究通过表达纯化的重组DHX33蛋白，结合细胞实验发现DHX33与转录因子AP-1相互作用，促进c-MYC基因转录，从而驱动结直肠癌的增殖和转移。重组DHX33的体外功能分析验证了其解旋酶活性在致癌通路中的关键作用。
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2. **文献名称**：*Structural insights into DHX33 helicase activity and its role in antiviral immunity*
**作者**：Liu X, et al.
**摘要**：研究利用重组DHX33蛋白解析其晶体结构，揭示了ATP结合域和解旋酶核心的构象变化机制。实验表明，DHX33通过识别病毒RNA并激活RIG-I信号通路，增强宿主抗病毒免疫反应。重组蛋白的功能缺失实验证实其关键结构域对免疫调控的必要性。
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3. **文献名称**：*DHX33 promotes glioblastoma progression via mTORC1 signaling activation*
**作者**：Wang H, et al.
**摘要**：通过重组DHX33蛋白的体外激酶实验和细胞模型，研究发现DHX33通过直接结合并激活mTORC1复合物，促进胶质母细胞瘤的代谢重编程和侵袭。研究强调了DHX33作为癌症治疗靶点的潜力。
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**备注**：以上文献信息为示例，实际文献需根据具体数据库(如PubMed、Web of Science)检索确认。如需进一步精准推荐，建议补充研究场景或具体应用方向(如结构解析、疾病机制或药物开发)。
**Background of DHX33 Recombinant Protein**
DHX33. a member of the DEAH-box helicase family, is an ATP-dependent RNA helicase involved in diverse cellular processes, including transcription, RNA splicing, translation, and innate immune responses. It plays critical roles in unwinding double-stranded RNA (dsRNA) or RNA-DNA hybrids, facilitating RNA metabolism and genomic stability. DHX33 is ubiquitously expressed and implicated in cell proliferation, apoptosis, and viral defense mechanisms. Dysregulation of DHX33 has been linked to cancers, neurodevelopmental disorders, and immune-related diseases, underscoring its biological significance.
Recombinant DHX33 protein is engineered through molecular cloning and heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce a purified, functional form of the enzyme. The protein typically retains conserved structural domains: an N-terminal domain for substrate recognition, a DEAH catalytic core for ATP hydrolysis, and a helicase domain for RNA binding and unwinding. These features enable its application in *in vitro* studies to dissect RNA helicase mechanisms, protein-RNA/DNA interactions, and nucleic acid remodeling processes.
Research utilizing DHX33 recombinant protein has advanced understanding of its role in stress granule formation, ribosome biogenesis, and antiviral signaling (e.g., via RIG-I-like receptor pathways). Additionally, it serves as a tool for screening small-molecule inhibitors targeting helicase activity in cancer or inflammation. In disease models, DHX33 has been shown to influence tumor progression by modulating oncogene expression and viral replication cycles, positioning it as a potential therapeutic target. Overall, DHX33 recombinant protein is pivotal for elucidating helicase-driven cellular mechanisms and developing targeted interventions in human diseases.
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