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Recombinant Human CPOX protein

  • 中文名: 原卟啉原氧化酶(CPOX)重组蛋白
  • 别    名: CPOX;CPO;CPX;Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
货号: PA1000-698DB
Price: ¥询价
数量:
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产品详情

纯度>95%SDS-PAGE.
种属Human
靶点CPOX
Uniprot NoP36551
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间111-454aa
氨基酸序列MGSSHHHHHHSSGLVPRGSHMGSTSLGRPEEEEDELAHRCSSFMAPPVTD LGELRRRPGDMKTKMELLILETQAQVCQALAQVDGGANFSVDRWERKEGG GGISCVLQDGCVFEKAGVSISVVHGNLSEEAAKQMRSRGKVLKTKDGKLP FCAMGVSSVIHPKNPHAPTIHFNYRYFEVEEADGNKQWWFGGGCDLTPTY LNQEDAVHFHRTLKEACDQHGPDLYPKFKKWCDDYFFIAHRGERRGIGGI FFDDLDSPSKEEVFRFVQSCARAVVPSYIPLVKKHCDDSFTPQEKLWQQL RRGRYVEFNLLYDRGTKFGLFTPGSRIESILMSLPLTARWEYMHSPSENS KEAEILEVLRHPRDWVR
预测分子量42 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.

参考文献

以下是关于 **CPOX重组蛋白** 的示例参考文献(注:以下内容为模拟生成,实际文献请通过学术数据库检索):

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1. **文献名称**:*Expression and Purification of Recombinant Human Coproporphyrinogen Oxidase (CPOX) in E. coli*

**作者**:Smith A, et al.

**摘要**:报道了通过大肠杆菌表达系统高效表达重组人CPOX蛋白的方法,并优化了纯化步骤,验证了其酶活性,为后续功能研究提供基础。

2. **文献名称**:*Structural Insights into CPOX Mutations Linked to Hereditary Coproporphyria*

**作者**:Johnson R, et al.

**摘要**:通过X射线晶体学解析了重组CPOX蛋白的三维结构,分析了与遗传性粪卟啉症相关的突变位点对酶催化功能的影响。

3. **文献名称**:*Functional Characterization of Recombinant CPOX Variants in Heme Biosynthesis*

**作者**:Lee S, et al.

**摘要**:利用昆虫细胞表达系统制备多种CPOX重组突变体,研究其酶动力学参数,揭示了特定氨基酸残基在血红素合成中的关键作用。

4. **文献名称**:*Development of a Yeast-Based System for High-Yield Production of CPOX*

**作者**:Garcia M, et al.

**摘要**:开发了一种基于酵母的重组CPOX蛋白高效表达平台,验证了其稳定性与生物活性,为卟啉症治疗研究提供了潜在工具。

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建议通过 **PubMed**、**Web of Science** 或 **Google Scholar** 检索关键词如 *"recombinant CPOX protein"* 或 *"coproporphyrinogen oxidase expression"* 获取最新文献。

背景信息

**Background of CPOX Recombinant Protein**

Coproporphyrinogen oxidase (CPOX) is a mitochondrial enzyme critical in the heme biosynthesis pathway, catalyzing the oxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IX. This step is essential for the production of heme, a vital cofactor in hemoglobin, cytochromes, and other hemoproteins. Mutations in the *CPOX* gene are associated with hereditary coproporphyria (HCP), a rare autosomal dominant metabolic disorder characterized by the accumulation of coproporphyrinogens, leading to neurovisceral and cutaneous symptoms.

Recombinant CPOX protein is produced using biotechnological platforms, such as *E. coli* or mammalian expression systems, to enable functional and structural studies. Its production allows researchers to investigate enzyme kinetics, substrate specificity, and the impact of disease-associated mutations. Recombinant CPOX is often engineered with affinity tags (e.g., His-tag) to facilitate purification and detection. Studies using this protein have clarified mechanisms underlying HCP pathogenesis, including how specific mutations reduce catalytic efficiency or destabilize the enzyme.

Additionally, recombinant CPOX serves as a tool for developing diagnostic assays, such as enzymatic activity tests in patient samples, and for high-throughput screening of potential therapeutic compounds. In drug discovery, it aids in identifying small molecules that enhance enzyme activity or stabilize mutant variants. Furthermore, recombinant CPOX is explored in gene therapy research to restore heme biosynthesis in deficient cells.

Structural analyses of recombinant CPOX, including X-ray crystallography and cryo-EM, have provided insights into its dimeric architecture and active-site dynamics, informing the design of targeted therapies. Overall, CPOX recombinant protein is pivotal in advancing understanding of porphyrias and developing innovative treatments for metabolic disorders linked to heme biosynthesis.

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