| 纯度 | >90%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | MPO |
| Uniprot No | P11247 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 139-718aa |
| 氨基酸序列 | VT CPPNDKYRTI TGHCNNRRSP TLGASNRAFV RWLPAEYEDG VSMPFGWTPG VNRNGFKVPL ARQVSNAIVR FPNDQLTKDQ ERALMFMQWG QFLDHDITLT PEPATRFSFF TGLNCETSCL QQPPCFPLKI PPNDPRIKNQ KDCIPFFRSC PACTRNNITI RNQINALTSF VDASGVYGSE DPLARKLRNL TNQLGLLAIN TRFQDNGRAL MPFDSLHDDP CLLTNRSARI PCFLAGDMRS SEMPELTSMH TLFVREHNRL ATQLKRLNPR WNGEKLYQEA RKIVGAMVQI ITYRDYLPLV LGPAAMKKYL PQYRSYNDSV DPRIANVFTN AFRYGHTLIQ PFMFRLNNQY RPTGPNPRVP LSKVFFASWR VVLEGGIDPI LRGLMATPAK LNRQNQIVVD EIRERLFEQV MRIGLDLPAL NMQRSRDHGL PGYNAWRRFC GLPQPSTVGE LGTVLKNLEL ARKLMAQYGT PNNIDIWMGG VSEPLEPNGR VGQLLACLIG TQFRKLRDGD RFWWENPGVF SKQQRQALAS ISLPRIICDN TGITTVSKNN IFMSNTYPRD FVSCNTLPKL NLTSWKET |
| 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MPO(髓过氧化物酶)重组蛋白研究的3篇参考文献示例：
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1. **文献名称**: *Expression and purification of recombinant human myeloperoxidase in Escherichia coli*
**作者**: Smith A, et al.
**摘要**: 该研究报道了在大肠杆菌中表达人源MPO的重组蛋白，并优化了纯化步骤。通过引入分子伴侣共表达系统提高可溶性蛋白产量，最终获得具有酶活性的MPO，为大规模制备提供了可行方案。
2. **文献名称**: *Structural characterization of recombinant myeloperoxidase propeptide and its role in protein processing*
**作者**: Johnson R, et al.
**摘要**: 文章利用哺乳动物细胞表达系统获得重组MPO，通过质谱和晶体学分析其前肽结构，揭示前肽在MPO正确折叠和血红素结合中的关键作用，为酶功能调控提供了新见解。
3. **文献名称**: *Functional analysis of recombinant MPO mutants in neutrophil-mediated inflammation models*
**作者**: Lee H, et al.
**摘要**: 研究通过昆虫细胞表达系统制备多种MPO突变体，验证其在体外炎症模型中的活性差异，发现特定结构域突变显著影响ROS(活性氧)生成能力，提示潜在的治疗靶点。
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注：以上文献为示例性内容，实际引用时需以具体数据库检索结果为准。建议通过PubMed或Web of Science以关键词“recombinant myeloperoxidase”查找最新研究。
Myeloperoxidase (MPO) is a heme-containing peroxidase predominantly expressed in neutrophils, playing a critical role in innate immunity. It catalyzes the production of hypochlorous acid (HOCl) from hydrogen peroxide and chloride ions, contributing to microbial killing and inflammatory responses. However, dysregulated MPO activity is linked to tissue damage in chronic inflammation, cardiovascular diseases, and neurodegenerative disorders. Recombinant MPO protein, engineered through heterologous expression systems (e.g., mammalian, insect, or bacterial cells), enables controlled study of its structure, enzymatic mechanisms, and pathological roles.
The production of recombinant MPO typically involves codon-optimized cDNA transfection into host cells, followed by purification via affinity chromatography. Challenges include preserving post-translational modifications (e.g., glycosylation) critical for its stability and activity, often necessitating mammalian expression systems. Recombinant MPO serves as a vital tool for drug discovery, allowing high-throughput screening of inhibitors targeting MPO-driven oxidative stress. It also aids in developing diagnostic assays for MPO-autoantibodies in autoimmune vasculitis.
Recent studies emphasize its dual role: while excessive MPO exacerbates tissue injury, its regulated activity supports pathogen clearance. Recombinant variants with modified enzymatic properties are being explored to dissect these context-dependent functions. Additionally, structural studies using recombinant MPO have revealed insights into its heme-binding site and substrate interaction, informing therapeutic design. Overall, recombinant MPO technology bridges basic research and clinical applications, offering avenues to mitigate MPO-related pathologies while harnessing its protective functions.
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