纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | LRPAP1 |
Uniprot No | P30533 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 35-357aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMYSREK NQPKPSPKRE SGEEFRMEKL NQLWEKAQRL HLPPVRLAEL HADLKIQERD ELAWKKLKLD GLDEDGEKEA RLIRNLNVIL AKYGLDGKKD ARQVTSNSLS GTQEDGLDDP RLEKLWHKAK TSGKFSGEEL DKLWREFLHH KEKVHEYNVL LETLSRTEEI HENVISPSDL SDIKGSVLHS RHTELKEKLR SINQGLDRLR RVSHQGYSTE AEFEEPRVID LWDLAQSANL TDKELEAFRE ELKHFEAKIE KHNHYQKQLE IAHEKLRHAE SVGDGERVSR SREKHALLEG RTKELGYTVK KHLQDLSGRI SRARHNEL |
预测分子量 | 40 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LRPAP1重组蛋白的3篇参考文献及其简要摘要:
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1. **文献名称**:*"Recombinant LRPAP1 inhibits β-amyloid uptake by modulating LRP1 trafficking in astrocytes"*
**作者**:Li et al. (2018)
**摘要**:该研究利用大肠杆菌表达的重组LRPAP1蛋白,证明其通过调控低密度脂蛋白受体相关蛋白1(LRP1)的内吞循环,显著抑制星形胶质细胞对β-淀粉样蛋白的摄取,为阿尔茨海默病的治疗提供了潜在靶点。
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2. **文献名称**:*"Structural and functional characterization of recombinant LRPAP1 in lipid metabolism regulation"*
**作者**:Zhang & Wang (2015)
**摘要**:作者通过哺乳动物细胞系统表达并纯化重组LRPAP1蛋白,结合X射线晶体学解析其结构,发现其通过结合LRP1的配体结合域,调控脂蛋白内化和胆固醇代谢,揭示了其在动脉粥样硬化中的分子机制。
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3. **文献名称**:*"LRPAP1 recombinant protein enhances Wnt/β-catenin signaling by stabilizing LRP5/6 receptors"*
**作者**:Chen et al. (2020)
**摘要**:研究显示,重组LRPAP1蛋白能够通过抑制泛素-蛋白酶体途径降解LRP5/6受体,增强Wnt/β-catenin信号通路活性,促进成骨细胞分化,为骨质疏松症的药物开发提供了新思路。
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(注:以上文献信息为模拟示例,实际引用时需核实真实存在的论文。)
LRPAP1 (Low-density lipoprotein receptor-related protein-associated protein 1), also known as RAP (receptor-associated protein), is a molecular chaperone critical for the biosynthesis and functional regulation of members of the low-density lipoprotein receptor (LDLR) family. This conserved 40 kDa protein, encoded by the LRPAP1 gene in humans, is primarily expressed in the endoplasmic reticulum (ER) and plays a pivotal role in ensuring the proper folding, trafficking, and ligand-binding activity of LDLR-related receptors, including LRP1. megalin, and VLDLR. By transiently binding to these receptors during their maturation, LRPAP1 prevents premature interaction with ligands or intracellular partners, thereby safeguarding receptor integrity and functionality.
Structurally, LRPAP1 consists of three tandemly arranged domains homologous to LDLR ligand-binding repeats, which facilitate its interaction with receptor cysteine-rich regions. Its chaperone activity is essential for maintaining cellular homeostasis, particularly in tissues involved in lipid metabolism, such as the liver and brain. Dysregulation of LRPAP1 has been implicated in several pathological conditions. For instance, reduced LRPAP1 expression correlates with impaired clearance of amyloid-β peptides in Alzheimer’s disease models, while mutations are linked to autosomal recessive disorders affecting lipid metabolism and cellular signaling pathways.
Recombinant LRPAP1 protein, typically produced in Escherichia coli or mammalian expression systems, retains the ability to bind LDLR family members in vitro. This recombinant form is widely utilized to study receptor-ligand interactions, modulate receptor activity in experimental models, and explore therapeutic strategies targeting cholesterol homeostasis or neurodegenerative diseases. Its stability and well-characterized functional properties make it a valuable tool for both basic research and drug development initiatives.
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