| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PAOX |
| Uniprot No | Q6QHF9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-649aa |
| 氨基酸序列 | MESTGSVGEA PGGPRVLVVG GGIAGLGAAQ RLCGHSAFPH LRVLEATARA GGRIRSERCF GGVVEVGAHW IHGPSRGNPV FQLAAEYGLL GEKELSQENQ LVETGGHVGL PSVSYASSGT SVSLQLVAEM ATLFYGLIDQ TREFLHAAET PVPSVGEYLK KEIGQHVARL CGHSAFPHLR VLEATARAGG RIRSERCFGG VVEVGAHWIH GPSRGNPVFQ LAAEYGLLGE KELSQENQLV ETGGHVGLPS VSYASSGASV SLQLVAEMAT LFYGLIDQTR EFLHAAETPV PSVGEYLKKE IGQHVAGWTE DEETRKLKLA VLNSFFNLEC CVSGTHSMDL VALAPFGEYT VLPGLDCTFS KGYQGLTNCM MAALPEDTVV FEKPVKTIHW NGSFQEAAFP GETFPVSVEC EDGDRFPAHH VIVTVPLGFL REHLDTFFDP PLPAEKAEAI RKIGFGTNNK IFLEFEEPFW EPDCQLIQLV WEDTSPLEDA APELQDAWFR KLIGFVVLPA FASVHVLCGF IAGLESEFME TLSDEEVLLC LTQVLRRVTG NPRLPAPKSV LRSRWHSAPY TRGSYSYVAV GSTGGDLDLL AQPLPADGAG AQLQILFAGE ATHRTFYSTT HGALLSGWRE ADRLLSLWAP QVQQPRPRL |
| 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PAOX(多胺氧化酶)重组蛋白的3篇代表性文献摘要概括：
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1. **文献名称**: *Heterologous expression and characterization of human polyamine oxidase*
**作者**: Vujcic S, et al.
**摘要**: 研究通过大肠杆菌系统重组表达了人源PAOX蛋白，并分析了其酶学特性，揭示了其对特定多胺底物的催化机制及生理功能。
2. **文献名称**: *Recombinant production of plant polyamine oxidase for industrial applications*
**作者**: Tavladoraki P, et al.
**摘要**: 报道了利用酵母表达系统高效生产植物来源的PAOX重组蛋白，优化了纯化工艺，并验证了其在生物催化领域的潜在应用价值。
3. **文献名称**: *Structural insights into PAOX catalysis through recombinant protein crystallography*
**作者**: Wu H, et al.
**摘要**: 通过重组表达并纯化PAOX蛋白，解析了其晶体结构，阐明了活性位点关键氨基酸残基在氧化反应中的作用机制。
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注：以上文献信息为示例性质，实际文献需通过学术数据库(如PubMed、Web of Science)检索确认。
PAOX (Primary Alcohol Oxidase) is a recombinant enzyme widely studied for its catalytic role in oxidizing primary alcohols to corresponding aldehydes, coupled with the reduction of molecular oxygen to hydrogen peroxide. Originally identified in methylotrophic yeast species like *Pichia pastoris* (now *Komagataella phaffii*), PAOX is a flavin adenine dinucleotide (FAD)-dependent enzyme localized in peroxisomes. Its native function involves methanol metabolism, enabling yeast to utilize methanol as a carbon source by oxidizing it to formaldehyde. This unique substrate specificity and robust activity under mild conditions have driven interest in its biotechnological applications.
Recombinant PAOX is typically produced through heterologous expression in microbial hosts, such as *E. coli* or *P. pastoris*, leveraging genetic engineering to enhance yield, stability, or substrate range. Its structure features a conserved FAD-binding domain and a substrate-binding pocket optimized for short-chain aliphatic alcohols. Beyond methanol conversion, engineered PAOX variants are explored for chiral synthesis, biosensors, and biocatalysis in organic chemistry, particularly for producing aldehydes—valuable intermediates in pharmaceuticals and fragrances.
Research on PAOX also addresses challenges like oxygen dependency, substrate inhibition, and enzyme longevity. Recent advances include fusion proteins, immobilization techniques, and directed evolution to improve industrial viability. Additionally, PAOX-based systems are utilized in synthetic biology for metabolic pathway engineering, enabling sustainable production of biofuels or fine chemicals. Its role in peroxisome biology further links it to studies on cellular oxidative stress and detoxification mechanisms. Overall, PAOX exemplifies how understanding microbial enzymes can bridge fundamental biochemistry and applied industrial innovation.
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