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Recombinant Human AOX1 protein

  • 中文名: 乙醛氧化酶1(AOX1)重组蛋白
  • 别    名: AOX1;AO;Aldehyde oxidase
货号: PA1000-8779
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点AOX1
Uniprot No Q06278
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 236-421aa
氨基酸序列FGSERMMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHAYNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHIISRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSRK
预测分子量 24.6kDa
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AOX1重组蛋白的3篇参考文献示例(内容为虚构,仅作格式参考):

1. **文献名称**: "Heterologous Expression and Characterization of Human AOX1 in *Pichia pastoris*"

**作者**: Zhang, L. et al.

**摘要**: 本研究利用毕赤酵母系统成功表达并纯化了具有催化活性的人源AOX1重组蛋白。通过优化培养条件和诱导策略,获得了高产量酶,并验证其催化醛类底物氧化的功能,为药物代谢研究提供了工具酶。

2. **文献名称**: "Structural Insights into the Substrate Specificity of Recombinant AOX1 through Crystallography"

**作者**: Müller, R. & Schmidt, T.

**摘要**: 通过X射线晶体学解析了重组AOX1蛋白的3D结构,揭示了其底物结合口袋的关键氨基酸残基。实验证实,突变特定位点可显著改变其对不同醛类化合物的催化效率,为理性设计AOX1变体奠定基础。

3. **文献名称**: "Application of Recombinant AOX1 in the Biocatalytic Synthesis of Pharmaceutical Intermediates"

**作者**: Gupta, S. & Patel, K.

**摘要**: 探讨了重组AOX1在体外催化合成药物中间体中的潜力。研究表明,该酶在非水相体系中仍保持活性,可高效转化多种芳香醛类化合物,展示了其在绿色化学中的应用价值。

(注:以上文献信息为模拟生成,实际引用时请以真实数据库检索结果为准。)

背景信息

Alcohol oxidase 1 (AOX1) is a key enzyme involved in methanol metabolism, primarily found in methylotrophic yeast species such as *Pichia pastoris* (reclassified as *Komagataella phaffii*). It catalyzes the oxidation of methanol to formaldehyde, a critical step in the methanol utilization pathway. AOX1 is localized in peroxisomes and requires molecular oxygen and flavin adenine dinucleotide (FAD) as a cofactor. Its activity is tightly regulated, with expression induced by methanol and repressed by glucose or ethanol.

Recombinant AOX1 refers to the engineered version of this protein produced through heterologous expression systems, often in *P. pastoris* itself or other microbial hosts like *E. coli*. The recombinant protein retains the enzymatic properties of native AOX1 but is optimized for higher yield, stability, or ease of purification. This is achieved via genetic modifications, such as codon optimization, promoter engineering (e.g., using the strong, methanol-inducible AOX1 promoter), or fusion tags (e.g., His-tags).

AOX1 has garnered significant interest in biotechnology due to its role in methanol-based fermentation processes. It serves as a pivotal tool in the production of recombinant proteins, where *P. pastoris* is employed as a cell factory. The enzyme’s ability to drive methanol metabolism enables high-density cell cultures, enhancing target protein yields. Beyond industrial applications, recombinant AOX1 is studied for its structural features (e.g., octameric quaternary structure) and as a model for understanding peroxisomal enzyme dynamics.

Recent advancements focus on engineering AOX1 variants with improved catalytic efficiency or thermostability, expanding its utility in synthetic biology and bioremediation. Challenges remain in balancing enzyme activity with host cell health, as methanol oxidation generates toxic byproducts like hydrogen peroxide. Overall, AOX1 exemplifies the intersection of microbial metabolism and biotechnological innovation.

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