| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CPO |
| Uniprot No | P36551 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 111-454aa |
| 氨基酸序列 | TSLGRPEEEE DELAHRCSSF MAPPVTDLGE LRRRPGDMKT KMELLILETQ AQVCQALAQV DGGANFSVDR WERKEGGGGI SCVLQDGCVF EKAGVSISVV HGNLSEEAAK QMRSRGKVLK TKDGKLPFCA MGVSSVIHPK NPHAPTIHFN YRYFEVEEAD GNKQWWFGGG CDLTPTYLNQ EDAVHFHRTL KEACDQHGPD LYPKFKKWCD DYFFIAHRGE RRGIGGIFFD DLDSPSKEEV FRFVQSCARA VVPSYIPLVK KHCDDSFTPQ EKLWQQLRRG RYVEFNLLYD RGTKFGLFTP GSRIESILMS LPLTARWEYM HSPSENSKEA EILEVLRHPR DWVR |
| 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3篇关于CPO(Coproporphyrinogen Oxidase，粪卟啉原氧化酶)重组蛋白的模拟参考文献示例(文献信息为虚构，仅供格式参考)：
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1. **文献名称**: "Heterologous Expression and Characterization of Recombinant CPO from *E. coli* for Heme Biosynthesis"
**作者**: Zhang, L. et al.
**摘要**: 本研究在大肠杆菌中成功表达并纯化了重组CPO蛋白，验证了其在血红素生物合成途径中的催化活性。通过酶动力学分析发现，重组CPO对底物粪卟啉原III的催化效率较天然酶提高2.3倍，为工业化生产血红素前体提供了新策略。
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2. **文献名称**: "Structural Insights into Human CPO Deficiency Mutations via Recombinant Protein Crystallography"
**作者**: Smith, J.R. & Tanaka, M.
**摘要**: 通过重组表达人源CPO蛋白并进行X射线晶体学分析，揭示了与遗传性卟啉症相关的CPO突变体(如R331W)的构象变化，阐明了其酶活性丧失的分子机制，为靶向药物开发提供了结构基础。
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3. **文献名称**: "Optimization of CPO Recombinant Production in *Pichia pastoris* for Biocatalytic Applications"
**作者**: Gómez, A. et al.
**摘要**: 在毕赤酵母中优化了重组CPO的分泌表达系统，实现了高产量(1.2 g/L)和稳定活性。该重组酶在体外催化体系中成功将粪卟啉原转化为原卟啉原IX，为卟啉类化合物的生物制造提供了高效工具。
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注：以上文献为模拟内容，实际研究中建议通过PubMed、Web of Science等数据库检索真实文献(关键词：Coproporphyrinogen Oxidase, recombinant expression, porphyrin biosynthesis)。
**Background of CPO Recombinant Protein**
Coproporphyrinogen oxidase (CPO), also known as HemF, is a mitochondrial enzyme critical in the heme biosynthesis pathway. It catalyzes the oxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IX, a key step preceding the formation of heme—a molecule essential for oxygen transport, energy production, and cellular metabolism. Genetic mutations in the *CPOX* gene, which encodes CPO, can lead to hereditary coproporphyria (HCP), a rare metabolic disorder characterized by the accumulation of toxic porphyrin precursors.
Recombinant CPO protein technology emerged to address the need for functional enzyme studies and therapeutic applications. Using genetic engineering, the *CPOX* gene is cloned and expressed in heterologous systems like *E. coli* or yeast, enabling large-scale production of purified, bioactive CPO. This approach overcomes challenges in isolating the enzyme from natural sources and ensures consistency in research and drug development.
In biomedicine, recombinant CPO holds promise for enzyme replacement therapy (ERT) in porphyrias. Preclinical studies suggest that administering functional CPO could mitigate porphyrin precursor accumulation, alleviating symptoms such as neurovisceral crises and photosensitivity. Additionally, recombinant CPO is used to study enzyme kinetics, substrate specificity, and inhibition mechanisms, aiding in the design of targeted therapies.
Industrial applications include biosensing and biocatalysis, leveraging CPO’s ability to modify porphyrin derivatives for producing high-value compounds. Challenges remain in optimizing protein stability, activity, and delivery methods for clinical use. Recent advances in protein engineering, such as site-directed mutagenesis and fusion tags, aim to enhance CPO’s functional properties.
Overall, CPO recombinant protein represents a convergence of metabolic research, therapeutic innovation, and biotechnological engineering, offering tools to unravel heme-related pathologies and develop precision treatments.
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