纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | LRP11 |
Uniprot No | Q86VZ4 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-450aa |
氨基酸序列 | MASVAQESAG SQRRLPPRHG ALRGLLLLCL WLPSGRAALP PAAPLSELHA QLSGVEQLLE EFRRQLQQER PQEELELELR AGGGPQEDCP GPGSGGYSAM PDAIIRTKDS LAAGASFLRA PAAVRGWRQC VAACCSEPRC SVAVVELPRR PAPPAAVLGC YLFNCTARGR NVCKFALHSG YSSYSLSRAP DGAALATARA SPRQEKDAPP LSKAGQDVVL HLPTDGVVLD GRESTDDHAI VQYEWALLQG DPSVDMKVPQ SGTLKLSHLQ EGTYTFQLTV TDTAGQRSSD NVSVTVLRAA YSTGGCLHTC SRYHFFCDDG CCIDITLACD GVQQCPDGSD EDFCQNLGLD RKMVTHTAAS PALPRTTGPS EDAGGDSLVE KSQKATAPNK PPALSNTEKR NHSAFWGPES QIIPVMPDSS SSGKNRKEES YIFESKGDGG GGEHPAPETG |
预测分子量 | 45 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3-4条关于LRP11重组蛋白的虚构参考文献示例(注:以下内容为模拟生成,非真实文献):
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1. **文献名称**: *LRP11 Recombinant Protein Promotes Cancer Cell Invasion via Wnt/β-catenin Signaling*
**作者**: Zhang Y, et al.
**摘要**: 本研究利用重组人LRP11蛋白处理结肠癌细胞,发现其通过激活Wnt/β-catenin信号通路增强癌细胞迁移和侵袭能力,提示LRP11可能作为结直肠癌治疗的潜在靶点。
2. **文献名称**: *Structural Characterization of LRP11 Extracellular Domain and Its Interaction with Apolipoprotein E*
**作者**: Tanaka K, et al.
**摘要**: 通过X射线晶体学解析LRP11胞外域重组蛋白的三维结构,揭示其与载脂蛋白E(ApoE)的结合位点,为研究LRP11在脂质代谢和阿尔茨海默病中的作用提供分子机制依据。
3. **文献名称**: *LRP11 Knockdown Using Recombinant shRNA Protein Nanoparticles Suppresses Glioblastoma Progression*
**作者**: Chen L, et al.
**摘要**: 开发基于重组LRP11-shRNA的纳米颗粒递送系统,证明靶向抑制LRP11可降低胶质母细胞瘤细胞增殖并诱导凋亡,为新型脑肿瘤疗法提供实验基础。
4. **文献名称**: *LRP11 Recombinant Protein Modulates TGF-β Signaling in Pulmonary Fibrosis*
**作者**: Gupta R, et al.
**摘要**: 在小鼠肺纤维化模型中,外源性LRP11重组蛋白通过调控TGF-β/Smad通路减轻纤维化进程,提示其在纤维化疾病中的保护性功能。
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如需真实文献,建议通过PubMed或Google Scholar检索关键词:**LRP11 recombinant protein**、**LRP11 function** 或 **LRP11 disease association**。
**Background of LRP11 Recombinant Protein**
LRP11 (Low-Density Lipoprotein Receptor-Related Protein 11) is a member of the LDL receptor (LDLR) family, a group of transmembrane proteins involved in diverse cellular processes, including lipid metabolism, cell signaling, and endocytosis. Unlike well-characterized family members like LDLR or LRP1. LRP11 remains relatively understudied, though emerging evidence suggests roles in intracellular trafficking, neuronal development, and cancer progression. Structurally, LRP11 contains conserved LDLR class A repeats, epidermal growth factor (EGF)-like domains, and a cytoplasmic tail with potential signaling motifs, hinting at its involvement in ligand binding and receptor-mediated pathways.
Recombinant LRP11 protein is engineered *in vitro* using expression systems such as mammalian cells (e.g., HEK293) or insect cells to ensure proper post-translational modifications. This purified protein retains functional domains, enabling researchers to study its biochemical interactions, structural properties, and mechanisms in controlled settings. Key applications include elucidating LRP11's interaction with ligands (e.g., lipids, extracellular matrix components), its role in cellular uptake or signaling cascades (e.g., Wnt/β-catenin or TGF-β pathways), and its implications in diseases.
Notably, LRP11 has been linked to cancers, including glioblastoma and prostate cancer, where aberrant expression correlates with tumor invasiveness or drug resistance. In neuroscience, it may influence synaptic plasticity or neurodegenerative disorders. The recombinant form serves as a critical tool for developing antibodies, screening therapeutic compounds, or validating *in silico* predictions. Despite its potential, gaps remain in understanding its precise physiological roles, making LRP11 recombinant protein a valuable resource for bridging molecular characterization and functional studies. Ongoing research aims to unravel its pathophysiological significance, offering insights into novel diagnostic or therapeutic strategies.
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