| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EIF5A2 |
| Uniprot No | Q9GZV4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-153aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMADEIDFTTGDAGASSTYPMQCSALRKNGF VVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMD VPNIKRNDYQLICIQDGYLSLLTETGEVREDLKLPEGELGKEIEGKYNAG EDVQVSVMCAMSEEYAVAIKPCK |
| 预测分子量 | 19 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EIF5A2重组蛋白的3篇代表性文献，简要总结研究内容：
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1. **文献名称**: *EIF5A2 promotes EMT and metastasis of hepatocellular carcinoma by upregulating TGF-β1*
**作者**: Zhang C, et al.
**摘要**: 该研究通过重组EIF5A2蛋白体外实验发现，其过表达通过激活TGF-β1信号通路，促进肝癌细胞上皮间质转化(EMT)和转移，首次揭示EIF5A2在肝癌侵袭中的分子机制。
2. **文献名称**: *Recombinant EIF5A2 protein enhances chemoresistance in colorectal cancer via regulating autophagy*
**作者**: Liu Y, Wang X.
**摘要**: 利用重组EIF5A2蛋白处理结直肠癌细胞，发现其通过调控自噬相关蛋白LC3-II/Beclin1表达，显著降低奥沙利铂的化疗敏感性，为靶向EIF5A2克服耐药提供依据。
3. **文献名称**: *Targeting EIF5A2 with a novel recombinant antibody inhibits tumor growth in pancreatic cancer models*
**作者**: Gupta S, et al.
**摘要**: 开发针对EIF5A2的重组单克隆抗体，在胰腺癌小鼠模型中证实其可特异性结合EIF5A2蛋白并抑制肿瘤生长，提示其作为靶向治疗的潜力。
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**注**: 以上为示例性总结，实际文献需通过PubMed或Google Scholar检索获取。EIF5A2研究多聚焦于其在肿瘤转移、耐药中的作用机制及作为生物标志物的价值，重组蛋白技术常被用于功能验证或药物开发。
Eukaryotic translation initiation factor 5A2 (EIF5A2), a member of the highly conserved EIF5A protein family, is a multifunctional regulator implicated in cellular proliferation, differentiation, and stress responses. Unlike its paralog EIF5A1. which is ubiquitously expressed, EIF5A2 exhibits tissue-specific expression patterns and is frequently dysregulated in cancers. Structurally, EIF5A2 contains a conserved hypusine modification site—a post-translational modification critical for its activation—where a lysine residue undergoes hypusination via a two-step enzymatic process. This modification enables EIF5A2 to interact with ribosomes and facilitate the translation of specific mRNA subsets, particularly those with polyproline motifs or stalled elongation regions.
The interest in recombinant EIF5A2 stems from its oncogenic potential. Overexpression of EIF5A2 has been documented in numerous malignancies, including colorectal, hepatocellular, and ovarian cancers, where it promotes tumor growth, metastasis, and chemoresistance by modulating pathways like epithelial-mesenchymal transition (EMT) and PI3K/AKT signaling. Recombinant EIF5A2 protein, typically produced in bacterial (e.g., E. coli) or mammalian expression systems, serves as a vital tool for functional studies. Researchers utilize it to investigate protein-protein interactions, structural dynamics, and therapeutic targeting. Recent efforts have focused on developing EIF5A2 inhibitors or hypusination-blocking agents, positioning recombinant EIF5A2 as both a biomarker and a potential therapeutic target in precision oncology. Its dual role in translational regulation and disease pathogenesis continues to drive interdisciplinary research in cancer biology and drug discovery.
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