| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EEF2 |
| Uniprot No | P13639 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-858aa |
| 氨基酸序列 | VNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLNFIKQSKDGAGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLGPAERAKKVEDMMKKLWGDRYFDPANGKFSKSATSPEGKKLPRTFCQLILDPIFKVFDAIMNFKKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGLVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKQRARYLAEKYEWDVAEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQIIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRKRKGLKEGIPALDNFLDKL |
| 预测分子量 | 96.2 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EEF2重组蛋白的模拟参考文献示例(仅供参考，实际文献需通过学术数据库查询)：
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1. **文献名称**: *Expression and Purification of Recombinant Human EEF2 in Escherichia coli*
**作者**: Smith J, et al.
**摘要**: 研究报道了在大肠杆菌中高效表达并纯化重组人源EEF2蛋白的方法，通过优化密码子使用和诱导条件获得高产量蛋白，并验证其体外翻译活性。
2. **文献名称**: *Structural Insights into EEF2 Dynamics during Protein Synthesis*
**作者**: Chen L, et al.
**摘要**: 利用重组EEF2蛋白的晶体结构解析，揭示了其在核糖体翻译延伸过程中的构象变化，阐明了GTP水解与mRNA易位的分子机制。
3. **文献名称**: *EEF2 Phosphorylation by EEF2K in Cancer Cell Survival*
**作者**: Wang Y, et al.
**摘要**: 通过重组EEF2蛋白与激酶EEF2K的体外实验，证明EEF2的磷酸化调控与肿瘤细胞在营养胁迫下的存活密切相关，为靶向治疗提供依据。
4. **文献名称**: *Recombinant EEF2 as a Tool for Neurodegenerative Disease Research*
**作者**: Gonzalez R, et al.
**摘要**: 研究利用重组EEF2蛋白探究其在阿尔茨海默病模型中的异常表达，发现EEF2功能障碍可能导致突触蛋白合成受损。
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**提示**：如需真实文献，建议在PubMed、Google Scholar等平台搜索关键词(如“recombinant EEF2 protein”或“eEF2 expression”)，并筛选近年发表的高影响力论文。
**Background of Recombinant EEF2 Protein**
Eukaryotic Elongation Factor 2 (EEF2) is a critical GTP-binding protein responsible for catalyzing the translocation of transfer RNA (tRNA) and messenger RNA (mRNA) during the elongation phase of protein synthesis. This 96 kDa protein, conserved across eukaryotes, plays an indispensable role in ribosomal movement along mRNA templates, ensuring efficient polypeptide chain elongation. Its activity is tightly regulated by post-translational modifications, notably phosphorylation at Thr56 by EEF2 kinase, which temporarily halts translation under stress conditions.
Recombinant EEF2 protein is engineered through heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to produce purified, functional EEF2 for research and therapeutic applications. By cloning the *EEF2* gene into expression vectors, scientists achieve high-yield production while retaining native conformational properties and enzymatic activity. This recombinant tool enables precise study of EEF2's molecular mechanisms, including its interactions with ribosomes, GTP hydrolysis dynamics, and regulatory pathways.
Research leveraging recombinant EEF2 has advanced understanding of cellular stress responses, cancer biology (where EEF2 dysregulation promotes tumor survival), and neurodegenerative diseases. It also serves as a substrate for kinase assays, a target for drug discovery, and a reference protein in structural studies (e.g., cryo-EM). Recent efforts explore its potential in developing translation-targeted therapies and diagnostics for pathologies linked to protein synthesis defects. The accessibility of recombinant EEF2 continues to drive innovations in both basic and translational bioscience.
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