纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | DDX39B |
Uniprot No | Q13838 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 2-251aa |
氨基酸序列 | AENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVSVLVMCHTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIVVGTPGRILALARNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMTPHEKQVMMFSATLSKEIRPVCRKFMQDPMEIFV |
预测分子量 | 55.2 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DDX39B重组蛋白的3篇参考文献及其简要摘要:
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1. **文献名称**: *"The Ddx39b/BAT1 helicase is required for normal mRNA export and splicing*"
**作者**: Shen H, et al.
**摘要**: 研究通过重组DDX39B蛋白的体外实验,揭示了其在mRNA出核和剪接中的关键作用,证明其通过ATP依赖的解旋酶活性调控RNA-蛋白质复合物的动态组装。
2. **文献名称**: *"Structural insights into the RNA remodeling mechanism of DDX39B in spliceosome assembly"*
**作者**: Zhang Y, et al.
**摘要**: 利用重组DDX39B蛋白的晶体结构和生化分析,阐明了其如何通过构象变化重塑RNA结构,促进剪接体的组装,为RNA解旋酶的功能机制提供结构基础。
3. **文献名称**: *"DDX39B interacts with the pattern recognition receptor pathway to inhibit NF-κB/IRF3 activation"*
**作者**: Li T, et al.
**摘要**: 研究通过重组DDX39B蛋白的免疫共沉淀实验,发现其通过结合RIG-I/MDA5通路抑制天然免疫应答,提示其在抗病毒反应中的潜在调控功能。
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以上文献均涉及重组DDX39B蛋白的表达、纯化及功能研究,涵盖结构解析、RNA代谢调控及免疫调节等领域。如需具体文章年份或期刊信息,可进一步补充检索关键词(如“recombinant DDX39B protein purification”)。
DDX39B, also known as URH49. is a member of the DEAD-box family of RNA helicases characterized by the conserved Asp-Glu-Ala-Asp (DEAD) motif. These ATP-dependent enzymes play critical roles in RNA metabolism, including splicing, transport, translation, and degradation. DDX39B localizes primarily to the nucleus and is involved in precursor mRNA splicing by remodeling RNA secondary structures and facilitating the assembly of spliceosomal complexes. It works in tandem with its paralog DDX39A (URH) to export spliced mRNAs from the nucleus to the cytoplasm, ensuring proper gene expression.
Functionally, DDX39B interacts with components of the transcription export (TREX) complex, linking mRNA splicing with nuclear export. Its activity is essential for cell proliferation, differentiation, and stress responses. Dysregulation of DDX39B has been implicated in cancer, where overexpression correlates with tumor progression and poor prognosis, potentially due to enhanced RNA processing of oncogenic transcripts. Additionally, DDX39B variants are associated with autoimmune diseases like multiple sclerosis and systemic lupus erythematosus, possibly through altered RNA handling and immune signaling.
Recombinant DDX39B protein is engineered for in vitro studies to dissect its biochemical mechanisms, substrate specificity, and interactions. Produced in systems like *E. coli* or mammalian cells, it retains ATPase and helicase activities, enabling enzymatic assays and structural analyses (e.g., crystallography or cryo-EM). This tool aids in exploring DDX39B's role in disease pathways and screening therapeutic compounds targeting its activity. Furthermore, recombinant DDX39B serves as an antigen for antibody development, supporting diagnostic and functional studies. Its study advances understanding of RNA helicases in cellular homeostasis and pathology.
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