纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | EN1 |
Uniprot No | Q05925 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-392aa |
氨基酸序列 | MEEQQPEPKS QRDSALGAAA AATPGGLSLS LSPGASGSSG SGSDGDSVPV SPQPAPPSPP AAPCLPPLAH HPHLPPHPPP PPPQHLAAPA HQPQPAAQLH RTTNFFIDNI LRPDFGCKKE QPPPQLLVAA AARGGAGGGG RVERDRGQTA AGRDPVHPLG TRAPGAASLL CAPDANCGPP DGSQPAAAGA GASKAGNPAA AAAAAAAAVA AAAAAAAAKP SDTGGGGSGG GAGSPGAQGT KYPEHGNPAI LLMGSANGGP VVKTDSQQPL VWPAWVYCTR YSDRPSSGPR TRKLKKKKNE KEDKRPRTAF TAEQLQRLKA EFQANRYITE QRRQTLAQEL SLNESQIKIW FQNKRAKIKK ATGIKNGLAL HLMAQGLYNH STTTVQDKDE SE |
预测分子量 | 40,1 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3篇关于EN1重组蛋白的虚构示例文献(仅供参考格式,实际文献需通过学术数据库检索):
1. **《重组EN1蛋白在胚胎神经发育中的功能研究》**
- 作者:Chen L, Wang Y, et al. (2022)
- 摘要:通过在大肠杆菌中表达重组EN1蛋白,研究其对小鼠胚胎神经管发育的调控作用,发现EN1通过Wnt信号通路影响神经前体细胞分化。
2. **《EN1重组蛋白纯化及其在癌症侵袭机制中的应用》**
- 作者:Kim S, Patel R, et al. (2021)
- 摘要:开发了一种高效纯化EN1重组蛋白的亲和层析方法,并证明其在乳腺癌细胞中通过调控MMP-9表达促进肿瘤转移。
3. **《EN1蛋白结构与DNA结合活性的体外分析》**
- 作者:Gomez A, Müller T, et al. (2020)
- 摘要:利用重组EN1蛋白的晶体结构解析,揭示其同源结构域与靶基因DNA序列的特异性结合机制,为神经退行性疾病治疗提供新靶点。
4. **《EN1重组蛋白在帕金森病模型中的神经保护作用》**
- 作者:Zhang H, et al. (2023)
- 摘要:通过体外细胞模型验证EN1重组蛋白对多巴胺能神经元的保护作用,提出其可能通过抑制氧化应激通路延缓帕金森病进展。
**注**:以上为模拟文献,实际研究中需以PubMed/Web of Science等平台检索真实文献,关键词建议:*"EN1 recombinant protein" "Engrailed-1"*。
**Background of EN1 Recombinant Protein**
The EN1 (Engrailed-1) recombinant protein is derived from the *EN1* gene, which encodes a homeodomain-containing transcription factor critical in embryonic development. EN1 plays a pivotal role in patterning the midbrain-hindbrain boundary during neurogenesis and regulates limb and skeletal development. Its expression is tightly controlled in spatial and temporal contexts, with dysregulation linked to developmental disorders and cancers, including medulloblastoma and breast cancer.
Recombinant EN1 protein is typically produced using prokaryotic (e.g., *E. coli*) or eukaryotic (e.g., mammalian or insect cell) expression systems. These systems enable large-scale production of the protein with post-translational modifications mimicking native forms, depending on the host. The protein is often fused with tags (e.g., His-tag, GST) to facilitate purification via affinity chromatography. Quality control involves SDS-PAGE, Western blotting, and functional assays to confirm structural integrity and bioactivity.
Research applications of EN1 recombinant protein include *in vitro* studies to dissect its DNA-binding properties, transcriptional regulation mechanisms, and interactions with signaling pathways like Wnt and Hedgehog. It is also used to generate antibodies, model developmental processes, and explore its oncogenic role in cancer cell lines. In therapeutic contexts, EN1 is investigated as a potential target for small-molecule inhibitors or immunotherapies, particularly in cancers with aberrant EN1 expression.
Despite its utility, challenges remain in maintaining protein stability, solubility, and functional consistency across batches. Advances in protein engineering and expression optimization continue to address these issues, enhancing its applicability in basic research and translational medicine.
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