纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | RNGTT |
Uniprot No | O60942 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-597aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMAHNKIP PRWLNCPRRG QPVAGRFLPL KTMLGPRYDS QVAEENRFHP SMLSNYLKSL KVKMGLLVDL TNTSRFYDRN DIEKEGIKYI KLQCKGHGEC PTTENTETFI RLCERFNERN PPELIGVHCT HGFNRTGFLI CAFLVEKMDW SIEAAVATFA QARPPGIYKG DYLKELFRRY GDIEEAPPPP LLPDWCFEDD EDEDEDEDGK KESEPGSSAS FGKRRKERLK LGAIFLEGVT VKGVTQVTTQ PKLGEVQQKC HQFCGWEGSG FPGAQPVSMD KQNIKLLDLK PYKVSWKADG TRYMMLIDGT NEVFMIDRDN SVFHVSNLEF PFRKDLRMHL SNTLLDGEMI IDRVNGQAVP RYLIYDIIKF NSQPVGDCDF NVRLQCIERE IISPRHEKMK TGLIDKTQEP FSVRNKPFFD ICTSRKLLEG NFAKEVSHEM DGLIFQPTGK YKPGRCDDIL KWKPPSLNSV DFRLKITRMG GEGLLPQNVG LLYVGGYERP FAQIKVTKEL KQYDNKIIEC KFENNSWVFM RQRTDKSFPN AYNTAMAVCN SISNPVTKEM LFEFIDRCTA ASQGQKRKHH LDPDTELMPP PPPKRPRPLT |
预测分子量 | 71 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. |
以下为假设性参考文献示例,供参考:
1. **文献名称**:*Purification and functional characterization of recombinant RNGTT for mRNA capping studies*
**作者**:Smith A, et al.
**摘要**:研究通过大肠杆菌表达系统成功纯化重组RNGTT蛋白,证实其在体外mRNA加帽过程中的酶活性,并分析其与转录延伸因子的相互作用。
2. **文献名称**:*Structural insights into the RNA-binding domain of RNGTT using X-ray crystallography*
**作者**:Lee H, et al.
**摘要**:解析重组RNGTT蛋白的晶体结构,揭示其RNA结合域的关键氨基酸残基,为靶向药物设计提供结构基础。
3. **文献名称**:*RNGTT knockdown and overexpression models reveal its role in leukemia cell proliferation*
**作者**:Garcia R, et al.
**摘要**:通过重组蛋白互补实验,证明RNGTT通过调控mRNA稳定性影响白血病细胞的周期进程,提示其作为潜在治疗靶点。
4. **文献名称**:*High-throughput screening of RNGTT inhibitors using a fluorescence-based capping assay*
**作者**:Chen Z, et al.
**摘要**:开发基于重组RNGTT蛋白的高通量筛选平台,鉴定多个小分子抑制剂,并验证其可阻断病毒mRNA加帽过程。
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注:以上文献为模拟示例,实际文献需通过PubMed/Google Scholar等平台检索关键词“RNGTT recombinant protein”或“RNA guanylyltransferase”。
**Background of RNGTT Recombinant Protein**
RNGTT (RNA guanylyltransferase and 5'-phosphatase), also known as capping enzyme, is a bifunctional protein critical for RNA processing in eukaryotic cells. It plays a central role in the maturation of mRNA by catalyzing the formation of the 5' cap structure, a hallmark of eukaryotic mRNA essential for stability, nuclear export, and translational initiation. The enzyme sequentially removes the γ-phosphate from the 5' triphosphate of nascent RNA (5'-phosphatase activity) and transfers a GMP moiety from GTP to the diphosphate RNA end (guanylyltransferase activity), forming the GpppN cap. This cap structure is further modified by methylation to generate the mature m7GpppN cap.
The recombinant RNGTT protein is engineered for in vitro applications, typically expressed in bacterial or mammalian systems to ensure proper folding and enzymatic activity. Its production enables detailed studies of RNA capping mechanisms, which are vital for understanding gene expression regulation, viral replication (as many viruses hijack host capping machinery), and developmental processes. Dysregulation of capping is linked to cancers, neurological disorders, and viral pathogenesis, making RNGTT a potential therapeutic target.
Recombinant RNGTT is widely used in biochemical assays, structural studies (e.g., crystallography), and functional genomics. Its availability has accelerated research into cap-snatching by influenza viruses and the development of cap analogs for mRNA-based vaccines and therapies. Furthermore, engineered variants or inhibitors of RNGTT are explored for modulating RNA stability or viral replication.
Overall, RNGTT recombinant protein serves as a key tool in molecular biology, bridging fundamental research with biotechnological and medical innovations.
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