| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PON1 |
| Uniprot No | P27169 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-355aa |
| 氨基酸序列 | MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIET GSEDLEILPNGLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLEL GITGSKFDVSSFNPHGISTFTDEDNAMYLLVVNHPDAKSTVELFKFQEEE KSLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLDPYLQSWEMYLGL AWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEK HANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPP ASEVLRIQNILTEEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKA LYCEL |
| 预测分子量 | 41 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PON1重组蛋白的3篇代表性文献示例(注：内容为模拟摘要，仅供参考)：
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1. **文献名称**：*Expression and characterization of recombinant human paraoxonase 1 (PON1) in Escherichia coli*
**作者**：Stevens RC, et al.
**摘要**：本研究成功在大肠杆菌中表达了重组人PON1蛋白，优化了可溶性表达条件，并通过亲和层析纯化获得高活性酶。重组PON1表现出与天然酶相似的酯酶活性，并证实其可水解有机磷化合物。
2. **文献名称**：*Structural insights into the mechanism of paraoxonase 1 activation by HDL*
**作者**：Gaidukov L, et al.
**摘要**：通过重组PON1与高密度脂蛋白(HDL)复合物的结构分析，揭示了HDL结合对PON1酶活性和稳定性的调控机制，为理解其抗动脉粥样硬化功能提供了分子基础。
3. **文献名称**：*Site-directed mutagenesis of recombinant PON1 to enhance organophosphate hydrolase activity*
**作者**：Aharoni A, et al.
**摘要**：利用定点突变技术改造重组PON1的活性位点，显著提高了其对有机磷毒物的水解效率，为开发基于PON1的解毒剂提供了实验依据。
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(提示：实际研究中建议通过PubMed或Web of Science检索最新文献，关键词如“recombinant PON1 protein”或“paraoxonase 1 expression”。)
Paraoxonase 1 (PON1) is a calcium-dependent esterase primarily associated with high-density lipoprotein (HDL) in humans. It plays a critical role in hydrolyzing oxidized lipids, organophosphates, and aromatic esters, contributing to antioxidant and anti-inflammatory functions. PON1’s enzymatic activity is linked to cardiovascular health, neuroprotection, and detoxification processes, with genetic polymorphisms influencing its expression and efficacy. Reduced PON1 activity is associated with atherosclerosis, diabetes, and neurodegenerative disorders, making it a biomarker for oxidative stress-related diseases.
Recombinant PON1 (rPON1) is produced using biotechnological platforms like bacterial (E. coli) or mammalian expression systems to overcome limitations of native protein purification, such as low yield and heterogeneity. The recombinant form allows for controlled production, structural modifications (e.g., site-directed mutagenesis), and functional studies to elucidate its catalytic mechanisms and therapeutic potential. For instance, engineered rPON1 variants with enhanced stability or substrate specificity are explored for detoxifying organophosphate pesticides or mitigating lipid peroxidation in vascular diseases.
Research on rPON1 also focuses on its "bioligase" property—a secondary function involving protein-protein interactions that may regulate HDL metabolism and immune responses. Challenges remain in maintaining its native conformation post-purification, as misfolding can reduce activity. Current applications span in vitro diagnostics, drug development, and enzyme replacement strategies. Additionally, animal models expressing human rPON1 help validate its protective roles in vivo. As a multifunctional protein, rPON1 represents a promising therapeutic target and a tool for studying oxidative stress pathways, though clinical translation requires further optimization of bioavailability and delivery systems.
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