纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | LCN8 |
Uniprot No | Q6JVE9-2 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-152aa |
氨基酸序列 | MEELDRQKIG GFWREVGVAS DQSLVLTAPK RVEGLFLTLS GSNLTVKVAY NSSGSCEIEK IVGSEIDSTG KFAFPGHREI HVLDTDYEGY AILRVSLMWR GRNFRVLKYF TRSLEDKDRL GFWKFRELTA DTGLYLAARP GRCAELLKEE LI |
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LCN8重组蛋白的示例参考文献(注:以下内容为示例,实际文献需根据具体研究查询):
1. **文献名称**:*"Expression and Functional Characterization of Recombinant Human LCN8 in Bacterial Systems"*
**作者**:Zhang Y, Liu X, Chen J.
**摘要**:该研究成功在大肠杆菌中表达了重组人源LCN8蛋白,并通过亲和层析纯化获得高纯度蛋白。功能实验表明,重组LCN8在体外具有结合铁离子的能力,可能参与炎症调控。
2. **文献名称**:*"LCN8 Recombinant Protein Attenuates Colitis in Mice by Modulating Gut Microbiota"*
**作者**:Wang H, Li T, Kim M.
**摘要**:研究利用重组LCN8蛋白治疗小鼠结肠炎模型,发现其通过调节肠道菌群平衡和抑制促炎因子(如TNF-α)的表达,显著减轻肠道炎症。
3. **文献名称**:*"Structural Insights into the Iron-Binding Properties of Recombinant LCN8"*
**作者**:Smith R, Patel K, Lee S.
**摘要**:通过X射线晶体学解析了重组LCN8的三维结构,揭示了其与铁离子结合的关键氨基酸残基,为开发基于LCN8的靶向药物提供理论依据。
4. **文献名称**:*"Recombinant LCN8 Enhances Neuronal Survival in a Parkinson’s Disease Model"*
**作者**:Gupta P, Sharma N, Singh R.
**摘要**:研究发现,重组LCN8蛋白能够通过激活抗氧化通路(如Nrf2),减少多巴胺能神经元氧化应激损伤,在帕金森病模型中表现出神经保护作用。
建议通过PubMed、Web of Science等数据库,以关键词“LCN8 recombinant protein”或“Lipocalin 8 expression”检索最新文献以获取准确信息。
LCN8 (Lipocalin 8) is a member of the lipocalin protein family, characterized by a conserved eight-stranded β-barrel structure that enables binding and transport of small hydrophobic molecules, such as lipids, steroids, and metabolites. This secreted glycoprotein is encoded by the LCN8 gene, which is evolutionarily conserved across vertebrates, suggesting critical physiological roles. While its specific biological functions remain less characterized compared to other lipocalins (e.g., LCN2 in iron metabolism or LCN1 in tear film stability), emerging studies implicate LCN8 in cellular processes like inflammation modulation, cell signaling, and tissue homeostasis. Its expression has been detected in reproductive tissues, skin, and certain cancers, though functional insights are still evolving.
Recombinant LCN8 protein is produced using biotechnological platforms, typically through expression in bacterial (e.g., *E. coli*) or mammalian cell systems, followed by purification via affinity chromatography. Engineered variants may include tags (e.g., His-tag) to facilitate isolation and detection. Research applications focus on elucidating LCN8's ligand interactions, receptor partnerships, and role in disease contexts. For instance, preliminary evidence suggests its involvement in cancer progression by influencing cell migration or survival pathways. Additionally, its potential as a biomarker or therapeutic target is under exploration, particularly in conditions linked to lipid dysregulation or immune responses.
Challenges in LCN8 recombinant production include maintaining proper post-translational modifications (e.g., glycosylation) for functional studies, necessitating tailored expression systems. Ongoing work aims to decode its mechanistic contributions to physiology and pathology, leveraging recombinant tools to bridge structural analysis with cellular assays. As a relatively understudied lipocalin, LCN8 represents an intriguing subject for both basic research and translational innovation.
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