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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AZU |
| Uniprot No | P20160 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-250aa |
| 氨基酸序列 | IVGGRKARPRQFPFLASIQNQGRHFCGGALIHARFVMTAASCFQSQNPGV STVVLGAYDLRRRERQSRQTFSISSMSENGYDPQQNLNDLMLLQLDREAN LTSSVTILPLPLQNATVEAGTRCQVAGWGSQRSGGRLSRFPRFVNVTVTP EDQCRPNNVCTGVLTRRGGICNGDGGTPLVCEGLAHGVASFSLGPCGRGP DFFTRVALFRDWIDGVLNNPGPGP |
| 预测分子量 | 26 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. |
以下为3篇关于AZU(Azurin)重组蛋白的模拟参考文献示例，供参考：
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1. **文献名称**：Recombinant Azurin Expression and Purification in E. coli
**作者**：Yamada T. et al.
**摘要**：研究通过大肠杆菌表达系统高效表达重组Azurin蛋白，优化纯化条件(如镍柱亲和层析)，并验证其结构完整性(圆二色谱分析)，为后续抗癌研究提供基础。
2. **文献名称**：Anticancer Activity of Azurin: Mechanism Exploration
**作者**：Fiorino A., et al.
**摘要**：探讨重组Azurin通过诱导肿瘤细胞凋亡(如激活p53通路)和抑制血管生成的抗肿瘤机制，体外实验显示其对乳腺癌细胞的高选择性抑制作用。
3. **文献名称**：Azurin as a Drug Delivery Carrier
**作者**：Krishnan S., et al.
**摘要**：构建Azurin-化疗药物(如阿霉素)融合蛋白，证明其通过靶向肿瘤细胞表面受体增强药物递送效率，动物实验显示抑瘤率提升且毒性降低。
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⚠️ **注**：以上文献为模拟示例，实际研究需通过PubMed、SciFinder或Web of Science等平台检索关键词(如“Recombinant Azurin”、“Azurin cancer therapy”)获取真实文献。
**Background of AZU (Azurin) Recombinant Protein**
Azurin, a small copper-containing redox protein (molecular weight ~14 kDa), is naturally produced by the bacterium *Pseudomonas aeruginosa*. It plays a role in bacterial electron transport and stress response. Structurally, azurin adopts a beta-barrel fold with a type 1 copper-binding site, enabling electron transfer activity. Its unique stability and cell-penetrating properties have drawn interest in biomedical research, particularly in cancer therapy.
In the 1990s, studies revealed azurin’s selective anticancer activity. It enters cancer cells via endocytosis, interacts with tumor suppressor p53. and induces apoptosis while sparing healthy cells. A 28-amino-acid peptide fragment (p28) derived from azurin further demonstrated anticancer potential by modulating cell cycle proteins. These findings positioned recombinant azurin as a promising therapeutic candidate.
Recombinant azurin is produced using *E. coli* or yeast expression systems, ensuring high purity and scalability. Beyond oncology, it is explored for antimicrobial applications due to its bacterial origin and redox properties. Additionally, its ability to deliver cargo molecules into cells has spurred research in drug delivery and diagnostics.
Despite preclinical success, challenges remain in optimizing pharmacokinetics and minimizing immunogenicity. Current research focuses on engineering azurin variants and hybrid molecules to enhance efficacy and specificity. Overall, AZU recombinant protein represents a multifunctional biomolecule bridging microbial biochemistry and translational medicine, with potential applications spanning cancer treatment, infection control, and biotechnology.
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