| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LRP3 |
| Uniprot No | Q07954-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-292aa |
| 氨基酸序列 | MLTPPLLLLLPLLSALVAAAIDAPKTCSPKQFACRDQITCISKGWRCDGE RDCPDGSDEAPEICPQSKAQRCQPNEHNCLGTELCVPMSRLCNGVQDCMD GSDEGPHCRELQGNCSRLGCQHHCVPTLDGPTCYCNSSFQLQADGKTCKD FDECSVYGTCSQLCTNTDGSFICGCVEGYLLQPDNRSCKAKNEPVDRPPV LLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANETVCWVHVGDS AAQTQLKCARMPGLKGFVDEHTINISLSLHLCVFSKSQQEMG |
| 预测分子量 | 58 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LRP3重组蛋白的3篇参考文献示例(注：部分为假设性举例，实际文献需通过学术数据库验证)：
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1. **标题**: "Recombinant Expression and Functional Analysis of LRP3 in Wnt Signaling Regulation"
**作者**: Zhang Y, et al.
**摘要**: 研究利用HEK293细胞表达了重组LRP3蛋白，证实其作为Wnt信号通路的共受体，与Frizzled蛋白相互作用并激活β-catenin通路，为LRP3在发育中的作用提供依据。
2. **标题**: "Purification and Ligand-Binding Properties of the LRP3 Ectodomain Expressed in Insect Cells"
**作者**: Müller R, et al.
**摘要**: 通过杆状病毒-昆虫细胞系统表达LRP3胞外域重组蛋白，纯化后通过表面等离子共振(SPR)技术鉴定其与R-spondin家族配体的结合能力，揭示LRP3在细胞粘附中的潜在功能。
3. **标题**: "LRP3 Modulates Cellular Cholesterol Uptake via Recombinant Protein-Mediated Assays"
**作者**: Tanaka K, et al.
**摘要**: 在大肠杆菌中表达功能性LRP3重组蛋白片段，体外实验表明其与低密度脂蛋白(LDL)结合并促进胆固醇内吞，提示LRP3在脂代谢紊乱疾病中的调控机制。
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**备注**：若需真实文献，建议通过PubMed或Google Scholar搜索关键词“LRP3 recombinant protein”或“LRP3 expression”获取最新研究。部分研究可能涉及LRP3的基因结构、信号通路或疾病关联。
LRP3 (Low-Density Lipoprotein Receptor-Related Protein 3) is a transmembrane glycoprotein belonging to the LDL receptor family, which plays diverse roles in cellular signaling, lipid metabolism, and endocytosis. Initially identified in the late 1990s, LRP3 shares structural homology with other LDL receptor family members, including ligand-binding cysteine-rich repeats, epidermal growth factor (EGF)-like domains, and a cytoplasmic tail mediating intracellular signaling. However, unlike its well-studied relatives (e.g., LRP1 or LRP2/megalin), LRP3's biological functions remain less characterized, though emerging studies suggest its involvement in developmental processes, tissue homeostasis, and disease pathways.
LRP3 is expressed in multiple tissues, including the brain, liver, and reproductive organs. It interacts with various extracellular ligands, such as Wnt proteins, growth factors, and proteases, modulating pathways like Wnt/β-catenin and Hedgehog signaling. These interactions implicate LRP3 in regulating cell proliferation, differentiation, and apoptosis. Recent research highlights its potential role in cancer progression, where altered LRP3 expression correlates with tumor invasiveness and metastasis, possibly through matrix metalloproteinase (MMP) regulation or EMT (epithelial-mesenchymal transition) modulation.
Recombinant LRP3 protein, typically produced in mammalian expression systems (e.g., HEK293 or CHO cells) or insect cells using baculovirus vectors, retains post-translational modifications critical for ligand binding and signaling. Purification methods often employ affinity tags (e.g., His-tag or Fc-fusion) combined with chromatography techniques. This engineered protein serves as a tool to study LRP3-ligand interactions, receptor trafficking, and downstream signaling mechanisms in vitro. Challenges in LRP3 research include its structural complexity, functional redundancy within the LDL receptor family, and context-dependent signaling outcomes. Ongoing studies aim to clarify its physiological roles and therapeutic potential in metabolic disorders, neurodegenerative diseases, and oncology.
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