| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | eno |
| Uniprot No | Q2YSE8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-434aa |
| 氨基酸序列 | MPIITDVYAREVLDSRGNPTVEVEVLTESGAFGRALVPSGASTGEHEAVELRDGDKSRYLGKGVTKAVENVNEIIAPEIIEGEFSVLDQVSIDKMMIALDGTPNKGKLGANAILGVSIAVARAAADLLGQPLYKYLGGFNGKQLPVPMMNIVNGGSHSDAPIAFQEFMILPVGATTFKESLRWGTEIFHNLKSILSKRGLETAVGDEGGFAPKFEGTEDAVETIIQAIEAAGYKPGEEVFLGFDCASSEFYENGVYDYSKFEGEHGAKRTAAEQVDYLEQLVDKYPIITIEDGMDENDWDGWKQLTERIGDRVQLVGDDLFVTNTEILAKGIENGIGNSILIKVNQIGTLTETFDAIEMAQKAGYTAVVSHRSGETEDTTIADIAVATNAGQIKTGSLSRTDRIAKYNQLLRIEDELFETAKYDGIKSFYNLDK |
| 预测分子量 | 54.0 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. |
以下是关于重组eno(烯醇酶)蛋白的参考文献示例，内容基于典型研究方向构建：
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1. **《Cloning and Expression of Streptococcus pneumoniae Enolase in Escherichia coli》**
- 作者：Zhang L, et al.
- 摘要：研究通过克隆肺炎链球菌的eno基因，在大肠杆菌中成功表达重组烯醇酶蛋白，并验证其作为潜在疫苗候选抗原的免疫原性，为抗肺炎链球菌感染提供新策略。
2. **《Immunogenicity of Candida albicans Recombinant Enolase in Murine Models》**
- 作者：Wang Y, et al.
- 摘要：通过重组技术表达白色念珠菌烯醇酶蛋白，证实其能诱导小鼠产生特异性抗体，并增强对系统性念珠菌感染的抵抗力，提示其在真菌疫苗开发中的潜力。
3. **《Recombinant Human α-Enolase as a Biomarker for Cancer Diagnosis》**
- 作者：Kim S, et al.
- 摘要：研究利用重组人源α-烯醇酶蛋白，开发高灵敏度ELISA检测方法，发现其在多种癌症患者血清中显著高表达，或可作为肿瘤诊断的新型生物标志物。
4. **《Characterization of Helicobacter pylori Enolase as a Virulence Factor》**
- 作者：Chen H, et al.
- 摘要：重组表达幽门螺杆菌烯醇酶蛋白，发现其通过结合宿主纤溶酶原促进细菌定植，揭示eno在胃黏膜损伤及感染进程中的关键作用。
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注：以上文献为示例，实际引用需以真实发表论文为准。
Eno (α-enolase) is a multifunctional protein encoded by the ENO1 gene, primarily recognized as a glycolytic enzyme catalyzing the conversion of 2-phosphoglycerate to phosphoenolpyruvate. Beyond its metabolic role, enolase exhibits "moonlighting" functions, participating in diverse cellular processes such as cell adhesion, immune regulation, and hypoxia response. It localizes not only in the cytoplasm but also on cell surfaces or in extracellular spaces, interacting with plasminogen, extracellular matrix components, and pathogens, implicating it in tissue remodeling, inflammation, and microbial pathogenesis.
Recombinant enolase (rEno) is engineered via heterologous expression systems (e.g., E. coli, yeast, or mammalian cells) to study its structure-function relationships or therapeutic potential. Its recombinant form retains enzymatic activity and ligand-binding properties, enabling applications in antibody production, drug discovery, and diagnostic assays. For instance, autoantibodies against enolase are biomarkers in autoimmune diseases, while pathogen-derived enolase (e.g., in Streptococcus or Candida) is investigated for vaccine development due to its immunogenicity.
In cancer research, rEno helps explore its paradoxical roles: as a tumor suppressor via metabolic regulation and as a pro-metastatic factor when surface-localized. Dysregulated enolase expression correlates with poor prognosis in multiple cancers, driving interest in targeting it with inhibitors or immunotherapies. However, challenges persist in understanding isoform-specific functions (ENO1/2/3) and context-dependent behavior. Recombinant technology facilitates these studies by providing pure, customizable protein variants, though post-translational modifications in native environments remain difficult to replicate. Overall, eno recombinant proteins serve as vital tools bridging basic research and translational medicine.
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