| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LPC |
| Uniprot No | P04083 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 5-346aa |
| 氨基酸序列 | SEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN |
| 预测分子量 | 42.3 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LPC(溶血磷脂酰胆碱)重组蛋白研究的3篇模拟参考文献(注：内容为示例，非真实文献)：
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1. **文献名称**: *Lysophosphatidylcholine enhances the stability and activity of recombinant membrane proteins in vitro*
**作者**: Smith J. et al.
**摘要**: 研究探讨LPC作为去污剂在重组膜蛋白(如GPCRs)表达和纯化中的应用，证明LPC能有效维持蛋白构象并提高其体外活性，为膜蛋白功能研究提供优化方案。
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2. **文献名称**: *Role of LPC in improving the solubility of recombinant amyloid-beta aggregates*
**作者**: Chen L. & Wang H.
**摘要**: 通过比较LPC与其他去污剂的效果，发现LPC可溶解重组表达的淀粉样蛋白β聚集体，并保留其抗原性，为阿尔茨海默病相关抗体开发提供技术支持。
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3. **文献名称**: *LPC-based liposomes for targeted delivery of recombinant therapeutic proteins*
**作者**: Kumar R. et al.
**摘要**: 开发了一种基于LPC的脂质体递送系统，用于包裹重组肿瘤坏死因子(TNF-α)，实验显示其能显著提高蛋白的细胞靶向性和体内稳定性。
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(注：如需真实文献，建议在PubMed或Google Scholar检索关键词“LPC recombinant protein”“lysophosphatidylcholine protein stabilization”)
**Background of LPC Recombinant Proteins**
LPC (Liquid Phase Chromatography) recombinant proteins are engineered biomolecules produced using advanced genetic and biotechnological methods. These proteins are synthesized by inserting target gene sequences into host organisms (e.g., bacteria, yeast, or mammalian cells), enabling large-scale production of specific proteins with high purity and functionality. The term "LPC" refers to the chromatographic techniques employed during purification, which are critical for isolating proteins from complex biological mixtures while maintaining their structural integrity and activity.
Recombinant protein technology emerged in the 1970s with breakthroughs in molecular cloning and gene expression systems. Over decades, innovations in expression vectors, codon optimization, and fermentation processes have enhanced protein yield and scalability. LPC-based purification methods, such as affinity chromatography, ion-exchange chromatography, and size-exclusion chromatography, became pivotal in downstream processing, ensuring proteins meet stringent quality standards for research and therapeutic applications.
LPC recombinant proteins are widely utilized in biomedical fields, including drug development (e.g., monoclonal antibodies, vaccines), diagnostics, and structural biology. Their role in therapeutics is particularly notable, with examples like insulin, growth hormones, and COVID-19 spike proteins produced via recombinant systems. Additionally, they serve as tools for studying protein interactions, signaling pathways, and disease mechanisms.
Challenges persist in optimizing expression systems for complex proteins (e.g., membrane proteins), minimizing post-translational modification discrepancies, and reducing production costs. Advances in synthetic biology, machine learning-driven protein design, and continuous chromatography systems are addressing these issues, paving the way for next-generation biologics. As personalized medicine and biopharmaceuticals expand, LPC recombinant proteins remain central to innovating healthcare solutions.
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