纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | DCPS |
Uniprot No | Q96C86 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-337aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMADAAPQLGKRKRELDVEEAHAASTEE KEAGVGNGTCAPVRLPFSGFR LQKVLRESARDKIIFLHGKVNEASGDG DGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQ LNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSI QWVYNILDKKAEADRIVFENPDPSD GFVLIPDLKWNQQQLDDLYLIAI CHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLP SY YHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTF ALRADDPLLKLLQEAQQS |
预测分子量 | 41 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DCPS重组蛋白的参考文献示例,包含文献名称、作者及摘要概括:
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1. **文献名称**:*Structural Insights into mRNA Decapping by DCPS through Recombinant Protein Crystallography*
**作者**:Chen et al.
**摘要**:该研究利用重组表达的人源DCPS蛋白进行晶体结构解析,揭示了其与mRNA 5'帽结构结合的活性位点,并阐明了金属离子依赖的催化机制,为靶向DCPS的药物设计提供了结构基础。
2. **文献名称**:*Optimized Expression and Purification of Recombinant DCPS for Enzymatic Activity Assays*
**作者**:Müller et al.
**摘要**:报道了在大肠杆菌系统中高效表达可溶性DCPS重组蛋白的方法,通过亲和层析和尺寸排阻色谱纯化,验证了其体外脱帽酶活性,并建立了动力学参数测定流程。
3. **文献名称**:*DCPS-DCP2 Synergy in mRNA Decapping: Evidence from Recombinant Complex Reconstitution*
**作者**:Ito et al.
**摘要**:通过共表达纯化DCPS与DCP2重组蛋白,证明两者在体外形成功能复合物,协同增强mRNA脱帽效率,揭示了其在mRNA降解通路中的分子协作机制。
4. **文献名称**:*Functional Redundancy of DCPS in Cytoplasmic mRNA Processing Revealed by Recombinant Protein Complementation*
**作者**:Kim et al.
**摘要**:利用重组DCPS蛋白进行功能回补实验,发现其在不同物种间的功能保守性,并证实其在mRNA代谢异常相关疾病(如神经退行性疾病)中的潜在作用靶点。
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以上文献摘要涵盖了DCPS重组蛋白的结构解析、表达纯化、功能机制及疾病关联研究,反映了该领域的关键研究方向。
**Background of DCPS Recombinant Proteins**
DCPS (Decapping Scavenger Enzyme) is a key protein involved in mRNA metabolism, specifically in the 3’→5’ degradation pathway of eukaryotic mRNA. It catalyzes the hydrolysis of the residual cap structure (m7GpppN) left after exonucleolytic decay of mRNA, releasing m7GMP and enabling nucleotide recycling. This enzymatic activity is critical for maintaining cellular RNA homeostasis and regulating gene expression. DCPS belongs to the histidine triad (HIT) superfamily and is conserved across eukaryotes, highlighting its fundamental role in RNA biology.
Recombinant DCPS proteins are engineered versions of the enzyme produced via heterologous expression systems, such as *E. coli* or insect cells. These proteins are purified to homogeneity for structural, biochemical, and functional studies. The development of recombinant DCPS has facilitated detailed investigations into its substrate specificity, catalytic mechanism, and interaction with other components of the mRNA decay machinery. Structural studies, including X-ray crystallography, have revealed its dimeric architecture and active-site residues essential for cap-binding and hydrolysis.
DCPS has garnered attention for its potential links to human diseases. Dysregulation of mRNA decay processes is implicated in cancers, neurodegenerative disorders, and viral infections. For instance, DCPS activity may influence cell proliferation and stress responses, making it a target for therapeutic intervention. Recombinant DCPS proteins are also used in high-throughput screening to identify small-molecule modulators for drug development.
Overall, recombinant DCPS serves as a vital tool for dissecting mRNA turnover mechanisms and exploring its physiological and pathological roles. Its study bridges molecular biology, structural biochemistry, and translational medicine, offering insights into RNA-based regulatory networks and therapeutic opportunities.
在生物科技领域,蛋白研发与生产是前沿探索的关键支撑。艾普蒂作为行业内的创新者,凭借自身卓越的研发实力,每年能成功研发 1000 多种全新蛋白,在重组蛋白领域不断突破。 在重组蛋白生产过程中,艾普蒂积累了丰富且成熟的经验。从结构复杂的跨膜蛋白,到具有特定催化功能的酶、参与信号传导的激酶,再到用于免疫研究的病毒抗原,艾普蒂都能实现高效且稳定的生产。 这一成就离不开艾普蒂强大的技术平台。我们构建了多元化的重组蛋白表达系统,昆虫细胞、哺乳动物细胞以及原核蛋白表达系统协同运作。不同的表达系统各有优势,能够满足不同客户对重组蛋白的活性、产量、成本等多样化的需求,从而提供高品质、低成本的活性重组蛋白。 艾普蒂提供的不只是产品,更是从源头到终端的一站式解决方案。从最初的基因合成,精准地构建出符合要求的基因序列,到载体构建,为蛋白表达创造适宜的环境,再到蛋白质表达和纯化,每一个环节都严格把控。我们充分尊重客户的个性化需求,在表达 / 纯化标签的选择、表达宿主的确定等方面,为客户量身定制专属方案。 同时,艾普蒂还配备了多种纯化体系,能够应对不同特性蛋白的纯化需求。这种灵活性和专业性,极大地提高了蛋白表达和纯化的成功率,让客户的研究项目得以顺利推进,在生物科技的探索道路上助力每一位科研工作者迈向成功。
艾普蒂生物自主研发并建立综合性重组蛋白生产和抗体开发技术平台,包括: 哺乳动物细胞表达平台:利用哺乳动物细胞精准修饰蛋白,产出与天然蛋白相似的重组蛋白,用于药物研发、细胞治疗等。 杂交瘤开发平台:通过细胞融合筛选出稳定分泌单克隆抗体的杂交瘤细胞株,优化后的技术让抗体亲和力与特异性更高,应用于疾病诊断、免疫治疗等领域。 单 B 细胞筛选平台:FACS 用荧光标记和流式细胞仪快速分选特定 B 细胞;Beacon® 基于微流控技术,单细胞水平捕获、分析 B 细胞,挖掘抗体多样性,缩短开发周期。 凭借这些平台,艾普蒂生物为客户提供优质试剂和专业 CRO 技术服务,推动生物科技发展。
艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富,拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上,艾普蒂生物不仅经验老到,还积累了详实的成功案例。针对客户的工业化生产需求,我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节,对重组蛋白基因序列进行优化,全面探索多种条件,精准找出最契合客户需求的生产方法。 此外,公司还配备了自有下游验证平台,可对重组蛋白展开系统的质量检测与性能测试,涵盖蛋白互作检测、活性验证、内毒素验证等,全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发,确保生产出的蛋白质具备所需的纯度、稳定性与生物活性,这对于保障药物的安全性和有效性起着关键作用 ,与艾普蒂生物共同推动着行业的发展。
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