| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OxLDL |
| Uniprot No | P78380 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 58-273aa |
| 氨基酸序列 | MQLSQVSDLLTQEQANLTHQKKKLEGQISARQQAEEASQESENELKEMIETLARKLNEKSKEQMELHHQNLNLQETLKRVANCSAPCPQDWIWHGENCYLFSSGSFNWEKSQEKCLSLDAKLLKINSTADLDFIQQAISYSSFPFWMGLSRRNPSYPWLWEDGSPLMPHLFRVRGAVSQTYPSGTCAYIQRGAVYAENCILAAFSICQKKANLRAQ |
| 预测分子量 | 28.7 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OxLDL(氧化低密度脂蛋白)重组蛋白的3篇代表性文献概览：
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1. **文献名称**：*LOX-1. a novel receptor for oxidized low-density lipoprotein*
**作者**：Sawamura T, et al.
**摘要**：首次发现LOX-1是内皮细胞上特异性识别OxLDL的受体，揭示其在动脉粥样硬化中调控炎症反应和泡沫细胞形成的机制。
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2. **文献名称**：*Oxidized LDL modulates Bax/Bcl-2 through the lectin-like Ox-LDL receptor-1 in vascular smooth muscle cells*
**作者**：Chen M, et al.
**摘要**：研究LOX-1受体介导的OxLDL信号通路如何通过调控Bax/Bcl-2比例诱导血管平滑肌细胞凋亡，促进动脉粥样硬化斑块不稳定性。
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3. **文献名称**：*Recombinant lectin-like oxidized low-density lipoprotein receptor-1 (LOX-1) as a potential therapeutic target for atherosclerosis*
**作者**：Yoshida H, et al.
**摘要**：探讨重组LOX-1蛋白在体外阻断OxLDL与细胞结合的作用，提出通过抑制LOX-1/OxLDL相互作用减轻血管炎症和斑块发展的治疗策略。
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这些研究聚焦于OxLDL及其受体的分子机制和潜在治疗应用，为动脉粥样硬化研究提供了关键理论基础。建议通过PubMed或Google Scholar检索具体文献的DOI以获取全文。
Oxidized low-density lipoprotein (OxLDL) is a chemically modified form of LDL cholesterol that plays a central role in the development of atherosclerosis. Under physiological conditions, LDL particles transport cholesterol through the bloodstream, but oxidative stress in arterial walls triggers lipid peroxidation and apolipoprotein B-100 modification, converting native LDL into OxLDL. This altered particle is recognized as a danger signal by the immune system, promoting endothelial dysfunction, foam cell formation, and chronic inflammation – key steps in atherosclerotic plaque progression.
Recombinant OxLDL proteins are engineered in vitro to mimic the biochemical properties of naturally oxidized LDL. They are typically produced by expressing the human apoB-100 protein in mammalian or bacterial expression systems, followed by controlled oxidation using chemical agents (e.g., copper ions) or enzymatic methods. This standardized approach ensures batch-to-batch consistency, overcoming the variability of naturally occurring OxLDL isolated from plasma.
These recombinant tools are vital for studying receptor-mediated interactions – particularly with scavenger receptors (SR-A, CD36. and LOX-1) – that mediate OxLDL uptake in macrophages and vascular cells. Researchers use them to investigate signaling pathways linking lipid metabolism to inflammatory responses, autophagy regulation, and cellular apoptosis. Pharmaceutical applications include screening potential anti-atherosclerosis compounds that inhibit OxLDL formation or block its pathological effects. Diagnostic developments focus on measuring OxLDL antibodies in serum as cardiovascular risk biomarkers.
Current challenges involve replicating the full spectrum of oxidation-derived epitopes present in vivo. Advanced versions now incorporate specific oxidation patterns (e.g., malondialdehyde- or 4-hydroxynonenal-modified lysine residues) to better model disease-relevant epitopes. As research tools, recombinant OxLDL proteins bridge mechanistic studies and therapeutic development in cardiovascular diseases and related metabolic disorders.
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