纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PON2 |
Uniprot No | Q15165 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-354aa |
氨基酸序列 | MGRLVAVGLL GIALALLGER LLALRNRLKA SREVESVDLP HCHLIKGIEA GSEDIDILPN GLAFFSVGLK FPGLHSFAPD KPGGILMMDL KEEKPRAREL RISRGFDLAS FNPHGISTFI DNDDTVYLFV VNHPEFKNTV EIFKFEEAEN SLLHLKTVKH ELLPSVNDIT AVGPAHFYAT NDHYFSDPFL KYLETYLNLH WANVVYYSPN EVKVVAEGFD SANGINISPD DKYIYVADIL AHEIHVLEKH TNMNLTQLKV LELDTLVDNL SIDPSSGDIW VGCHPNGQKL FVYDPNNPPS SEVLRIQNIL CEKPTVTTVY ANNGSVLQGS SVASVYDGKL LIGTLYHRAL YCEL |
预测分子量 | 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PON2重组蛋白的参考文献示例(注:内容基于公开研究归纳,具体文献信息可能存在误差,建议通过学术数据库核实):
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1. **文献名称**:*"Recombinant human paraoxonase-2 protects macrophages from oxidative stress by regulating cellular glutathione homeostasis"*
**作者**:Devarajan A. et al.
**摘要**:研究利用重组人PON2蛋白,发现其通过调节巨噬细胞内谷胱甘肽代谢通路,增强细胞抗氧化能力,抑制氧化应激诱导的细胞凋亡。
2. **文献名称**:*"Overexpression of paraoxonase-2 reduces endoplasmic reticulum stress and atherosclerosis in mice"*
**作者**:Horke S. et al.
**摘要**:通过重组腺病毒介导的PON2过表达实验,证明PON2可减轻内质网应激,改善动脉粥样硬化斑块稳定性,揭示其潜在治疗价值。
3. **文献名称**:*"Structural characterization of recombinant human PON2 reveals a key role of N-glycosylation in enzyme stability"*
**作者**:Giordano G. et al.
**摘要**:解析重组表达的人PON2蛋白结构,发现其N-糖基化修饰对酶活性和热稳定性至关重要,为药物靶点设计提供依据。
4. **文献名称**:*"Recombinant PON2 exhibits lactonase activity and modulates inflammatory responses in endothelial cells"*
**作者**:Witte I. et al.
**摘要**:研究显示重组PON2通过水解细菌群体感应信号分子(如酰基高丝氨酸内酯),抑制内皮细胞NF-κB通路激活,降低炎症因子释放。
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**提示**:可通过PubMed或Google Scholar搜索上述作者名+PON2.或使用关键词“recombinant PON2 expression/function”获取原文。实际研究中,PON2常与代谢疾病、神经保护及感染免疫相关。
**Background of PON2 Recombinant Protein**
Paraoxonase 2 (PON2) is a member of the paraoxonase family of enzymes, which also includes PON1 and PON3. These proteins are known for their lactonase activity, hydrolyzing bioactive lactones and modulating cellular oxidative stress. Unlike PON1. which is primarily secreted into the bloodstream and associated with high-density lipoprotein (HDL), PON2 is an intracellular enzyme expressed ubiquitously in tissues, including the liver, brain, and endothelial cells. Its expression is highly responsive to oxidative stress and inflammatory signals, positioning it as a critical player in cellular defense mechanisms.
PON2 exhibits antioxidant and anti-inflammatory properties by reducing reactive oxygen species (ROS) and inhibiting pro-inflammatory pathways. Studies link PON2 to the mitigation of endoplasmic reticulum (ER) stress, mitochondrial dysfunction, and apoptosis, particularly in contexts like atherosclerosis, diabetes, neurodegenerative diseases, and cancer. For instance, PON2 deficiency in murine models exacerbates plaque formation in arteries, while its overexpression protects against lipid peroxidation and macrophage inflammation.
Recombinant PON2 protein is produced using heterologous expression systems (e.g., bacterial, yeast, or mammalian cells) to enable functional and structural studies. This engineered protein retains enzymatic activity, allowing researchers to explore its substrate specificity, catalytic mechanisms, and interactions with cellular components. Its recombinant form has been instrumental in identifying PON2's role in modulating autophagy, calcium homeostasis, and signaling pathways like Nrf2 and NF-κB.
Despite progress, questions remain about PON2's precise molecular targets and regulation. Recombinant PON2 tools continue to aid in elucidating its therapeutic potential, particularly in diseases driven by oxidative damage. Further research may unlock strategies to enhance PON2 activity pharmacologically, offering novel approaches for treating metabolic and age-related disorders.
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