| 纯度 | 95 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | A1AT |
| Uniprot No | P08473 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-418aa |
| 氨基酸序列 | EDPQGDAAQK TDTSHHDQDH PTFNKITPNL AEFAFSLYRQ LAHQSNSTNI FFSPVSIATA FAMLSLGTKA DTHDEILEGL NFNLTEIPEA QIHEGFQELL RTLNQPDSQL QLTTGNGLFL SEGLKLVDKF LEDVKKLYHS EAFTVNFGDT EEAKKQINDY VEKGTQGKIV DLVKELDRDT VFALVNYIFF KGKWERPFEV KDTEEEDFHV DQVTTVKVPM MKRLGMFNIQ HCKKLSSWVL LMKYLGNATA IFFLPDEGKL QHLENELTHD IITKFLENED RRSASLHLPK LSITGTYDLK SVLGQLGITK VFSNGADLSG VTEEAPLKLS KAVHKAVLTI DEKGTEAAGA MFLEAIPMSI PPEVKFNKPF VFLMIEQNTK SPLFMGKVVN PTQK |
| 预测分子量 | 44 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A1AT重组蛋白的3-4篇模拟参考文献的简要概括(注：文献为虚拟示例，仅供格式参考)：
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1. **文献名称**：*High-yield production of recombinant human alpha-1 antitrypsin in E. coli using solubility-enhancing tags*
**作者**：Zhang Y. et al. (2015)
**摘要**：研究报道通过在大肠杆菌表达系统中融合溶解度增强标签(如SUMO标签)，显著提高重组A1AT的可溶性表达水平。纯化后的蛋白经体外验证，显示与天然A1AT相似的弹性蛋白酶抑制活性，为低成本生产治疗性A1AT提供了新策略。
2. **文献名称**：*Pichia pastoris expression system for glycosylated alpha-1 antitrypsin: Functional characterization and comparison to plasma-derived protein*
**作者**：Lee S. et al. (2018)
**摘要**：利用毕赤酵母表达系统成功获得糖基化修饰的重组A1AT。通过质谱分析确认其糖基化模式，并与血浆来源的A1AT进行功能对比，证实重组蛋白在抑制中性粒细胞弹性蛋白酶活性和抗炎作用上的等效性。
3. **文献名称**：*Inhalable nanoparticle-encapsulated recombinant A1AT mitigates lung inflammation in emphysema models*
**作者**：Brown K. et al. (2022)
**摘要**：开发了一种可吸入纳米颗粒递送系统，用于肺部靶向释放重组A1AT。在慢性阻塞性肺病(COPD)小鼠模型中，该制剂显著降低肺组织炎症因子水平，并延长蛋白活性，提示其作为新型吸入疗法的潜力。
4. **文献名称**：*CRISPR/Cas9-engineered CHO cells for high-efficiency production of recombinant alpha-1 antitrypsin*
**作者**：Smith J. et al. (2020)
**摘要**：通过CRISPR/Cas9技术优化CHO细胞系，敲除蛋白酶基因以减少重组A1AT的降解。优化后的细胞系产量提高3倍，且蛋白稳定性增强，为规模化生产符合临床标准的A1AT奠定基础。
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以上为虚拟文献示例，实际研究中请通过PubMed、Web of Science等平台检索真实文献。
Alpha-1 Antitrypsin (A1AT) is a serine protease inhibitor primarily synthesized in the liver, playing a critical role in protecting tissues from neutrophil-derived proteases such as elastase. Its main function is to regulate enzyme activity during inflammatory responses, particularly in the lungs, where uncontrolled elastase activity can lead to emphysema and chronic obstructive pulmonary disease (COPD). A1AT deficiency (AATD) is an autosomal codominant genetic disorder caused by mutations in the SERPINA1 gene, most notably the Z variant (Glu342Lys), which promotes protein misfolding and aggregation within hepatocytes. This results in both reduced circulating A1AT levels (predisposing to lung damage) and liver disease due to intracellular accumulation.
Recombinant A1AT (rA1AT) has been developed as a therapeutic alternative to plasma-derived A1AT augmentation therapy. Produced via genetic engineering in microbial (e.g., *E. coli*, yeast) or mammalian cell systems, recombinant forms aim to overcome limitations of plasma-derived products, including supply shortages and pathogen transmission risks. Expression systems influence post-translational modifications; mammalian cells (e.g., CHO cells) enable proper glycosylation critical for stability and function, whereas microbial systems offer cost-effective production but lack human-like glycosylation.
Clinically, rA1AT is investigated for both replacement therapy in AATD and broader applications. While plasma-derived A1AT remains standard care, recombinant versions show promise in preclinical models for reducing lung inflammation and protease imbalance. Emerging research explores engineered variants with enhanced stability, prolonged half-life (via PEGylation or Fc fusion), or modified activity profiles. Challenges include optimizing production yields, ensuring biological equivalence to native A1AT, and addressing immunogenicity risks. Beyond AATD, rA1AT is being studied for its anti-inflammatory and immunomodulatory properties in conditions like acute respiratory distress syndrome (ARDS), diabetes, and ischemia-reperfusion injury, highlighting its multifaceted therapeutic potential.
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