| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EEF1G |
| Uniprot No | P26641 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-437aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMAAGTLYTYPENWRAFKALIAAQYSGA QVRVLSAPPHFHFGQTNRTPEFLRKFPAGKVPAFEGDDGFCVFESNAIAY YVSNEELRGSTPEAAAQVVQWVSFADSDIVPPASTWVFPTLGIMHHNKQA TENAKEEVRRILGLLDAYLKTRTFLVGERVTLADITVVCTLLWLYKQVLE PSFRQAFPNTNRWFLTCINQPQFRAVLGEVKLCEKMAQFDAKKFAETQPK KDTPRKEKGSREEKQKPQAERKEEKKAAAPAPEEEMDECEQALAAEPKAK DPFAHLPKSTFVLDEFKRKYSNEDTLSVALPYFWEHFDKDGWSLWYSEYR FPEELTQTFMSCNLITGMFQRLDKLRKNAFASVILFGTNNSSSISGVWVF RGQELAFPLSPDWQVDYESYTWRKLDPGSEETQTLVREYFSWEGAFQHVG KAFNQGKIFK |
| 预测分子量 | 53 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EEF1G重组蛋白的3篇参考文献示例(内容为虚构，仅作格式参考)：
1. **《Recombinant expression and functional characterization of human EEF1G in protein biosynthesis》**
- 作者：Zhang L, et al.
- 摘要：研究成功在大肠杆菌中表达并纯化了重组人源EEF1G蛋白，证实其在体外翻译系统中对延长因子复合物(eEF1B)的组装及氨基酸-tRNA转运的关键作用。
2. **《Structural insights into EEF1G's role in cancer metastasis through recombinant protein crystallography》**
- 作者：Kim S, et al.
- 摘要：通过重组EEF1G蛋白的晶体结构解析，揭示了其与肿瘤相关蛋白(如β-catenin)的互作界面，为靶向EEF1G的癌症治疗策略提供结构基础。
3. **《EEF1G recombinant protein as a novel biomarker for neurodegenerative diseases》**
- 作者：Wang Y, et al.
- 摘要：利用重组EEF1G蛋白开发特异性抗体，发现其在阿尔茨海默病患者脑脊液中异常聚集，提示其作为神经退行性疾病标志物的潜力。
注：以上文献信息为示例，实际文献需通过PubMed、Web of Science等数据库检索确认。
EEF1G (Eukaryotic Translation Elongation Factor 1 Gamma) is a critical subunit of the eukaryotic elongation factor 1 complex (eEF1), which plays a central role in protein synthesis. The eEF1 complex, composed of subunits α, β, γ, and δ, facilitates the delivery of aminoacyl-tRNAs to the ribosome during the elongation phase of translation. Specifically, EEF1G serves as a structural scaffold that stabilizes the complex and mediates interactions between other subunits, such as EEF1A (responsible for GTP-dependent tRNA recruitment) and EEF1B2 (a guanine nucleotide exchange factor). Its conserved structural domains, including lipid-binding motifs and protein interaction sites, underscore its functional importance in translational fidelity and cellular homeostasis.
Recombinant EEF1G protein is produced using expression systems like *E. coli* or mammalian cells, often fused with tags (e.g., His-tag) for purification via affinity chromatography. This engineered protein enables detailed studies of eEF1 complex assembly, tRNA-ribosome dynamics, and elongation regulation. Beyond its canonical role, EEF1G has been implicated in non-translational processes, such as cytoskeletal organization, apoptosis, and viral replication. Dysregulation of EEF1G expression is associated with cancers, neurodegenerative disorders, and metabolic diseases, making it a potential biomarker or therapeutic target. Recombinant variants are also utilized in drug screening, structural biology (e.g., cryo-EM studies), and diagnostic assays. Research on EEF1G continues to unravel its multifunctional nature, bridging fundamental mechanisms of translation with broader cellular pathophysiology.
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