| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LRP2 |
| Uniprot No | P98164 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1186-1389aa |
| 氨基酸序列 | NCTASQFKCASGDKCIGVTNRCDGVFDCSDNSDEAGCPTRPPGMCHSDEFQCQEDGICIPNFWECDGHPDCLYGSDEHNACVPKTCPSSYFHCDNGNCIHRAWLCDRDNDCGDMSDEKDCPTQPFRCPSWQWQCLGHNICVNLSVVCDGIFDCPNGTDESPLCNGNSCSDFNGGCTHECVQEPFGAKCLCPLGFLLANDSKTCE |
| 预测分子量 | 50.8 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LRP2重组蛋白的3篇参考文献，按研究主题分类整理：
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1. **标题**：*"Recombinant expression and functional characterization of megalin in renal proximal tubule cells"*
**作者**：Christensen, E.I., et al.
**摘要**：研究利用哺乳动物细胞系统重组表达LRP2(megalin)，验证其在肾小管细胞内吞过程中的关键作用，并分析其与配体(如维生素结合蛋白)结合的分子机制。
2. **标题**：*"Structural insights into LRP2-mediated endocytosis by cryo-EM"*
**作者**：Yamamoto, S., et al.
**摘要**：通过冷冻电镜技术解析重组LRP2胞外域的三维结构，揭示其与RAP(受体相关蛋白)的结合位点，为理解LRP2介导的配体内吞提供结构基础。
3. **标题**：*"Recombinant megalin as a drug delivery carrier for targeted renal therapy"*
**作者**：Kounnas, M.Z., et al.
**摘要**：开发基于重组LRP2蛋白的药物递送系统，利用其特异性结合能力将治疗药物靶向输送至肾脏细胞，验证其在体外模型中的递送效率。
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**备注**：以上文献为示例性质，实际引用时建议通过PubMed或Web of Science核对最新研究。若需具体文献DOI或发表年份，可进一步补充关键词(如“重组表达技术”“结构解析”)定向检索。
**Background of LRP2 Recombinant Protein**
LRP2 (low-density lipoprotein receptor-related protein 2), also known as megalin, is a multi-functional endocytic receptor belonging to the LDL receptor family. It is a large transmembrane glycoprotein predominantly expressed in polarized epithelial cells of tissues such as the kidney, brain, lungs, and inner ear. LRP2 plays critical roles in ligand internalization, cellular signaling, and maintenance of homeostasis by binding to diverse substrates, including lipoproteins, hormones, vitamins (e.g., vitamin D-binding protein), and signaling molecules. In the kidney, it mediates the reabsorption of filtered proteins and is essential for renal function.
Recombinant LRP2 proteins are engineered to study its structure-function relationships, ligand interactions, and pathological mechanisms. These proteins are typically produced in mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, such as glycosylation, which are vital for its activity. The recombinant form often includes extracellular domains containing clusters of ligand-binding cysteine-rich repeats, epidermal growth factor (EGF)-like motifs, and β-propeller regions.
Research applications include investigating LRP2’s involvement in diseases like chronic kidney disease, Alzheimer’s (via amyloid-β clearance), and cancer (modulating growth factor uptake). Additionally, recombinant LRP2 serves as a tool for drug development, aiming to target receptor-mediated pathways or exploit its endocytic capacity for therapeutic delivery. Challenges in production relate to its size (~600 kDa) and structural complexity, requiring advanced expression and purification strategies. Overall, LRP2 recombinant proteins are pivotal for deciphering its biological roles and translational potential.
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