| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AAT1 |
| Uniprot No | P24298 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-496aa |
| 氨基酸序列 | ASSTGDRSQAVRHGLRAKVLTLDGMNPRVRRVEYAVRGPIVQRALELEQELRQGVKKPFTEVIRANIGDAQAMGQRPITFLRQVLALCVNPDLLSSPNFPDDAKKRAERILQACGGHSLGAYSVSSGIQLIREDVARYIERRDGGIPADPNNVFLSTGASDAIVTVLKLLVAGEGHTRTGVLIPIPQYPLYSATLAELGAVQVDYYLDEERAWALDVAELHRALGQARDHCRPRALCVINPGNPTGQVQTRECIEAVIRFAFEERLFLLADEVYQDNVYAAGSQFHSFKKVLMEMGPPYAGQQELASFHSTSKGYMGECGFRGGYVEVVNMDAAVQQQMLKLMSVRLCPPVPGQALLDLVVSPPAPTDPSFAQFQAEKQAVLAELAAKAKLTEQVFNEAPGISCNPVQGAMYSFPRVQLPPRAVERAQELGLAPDMFFCLRLLEETGICVVPGSGFGQREGTYHFRMTILPPLEKLRLLLEKLSRFHAKFTLEYS |
| 预测分子量 | 56.5 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AAT1重组蛋白的3篇参考文献示例(内容为模拟概括，仅供参考)：
1. **文献名称**：*Expression and characterization of recombinant human alpha-1 antitrypsin in transgenic rice cell culture*
**作者**：Huang N, et al.
**摘要**：研究利用转基因水稻细胞表达重组人AAT1.优化培养条件提高蛋白产量，并验证其对中性粒细胞弹性蛋白酶的抑制活性。
2. **文献名称**：*Production of functional recombinant human alpha-1 antitrypsin in Saccharomyces cerevisiae*
**作者**：Li H, et al.
**摘要**：通过酵母表达系统(酿酒酵母)成功生产具有生物活性的重组AAT1.分析其糖基化修饰对蛋白稳定性和功能的影响。
3. **文献名称**：*A novel purification strategy for recombinant alpha-1 antitrypsin using affinity chromatography*
**作者**：Gomes AR, et al.
**摘要**：开发一种基于亲和层析的新型纯化方法，高效分离重组AAT1.并通过质谱和功能实验证明其高纯度和抗炎活性。
4. **文献名称**：*Recombinant AAT1 mitigates lung injury in a murine emphysema model*
**作者**：Song J, et al.
**摘要**：评估重组AAT1在肺气肿小鼠模型中的治疗效果，显示其通过抑制蛋白酶活性和减少炎症反应改善肺部病理。
---
注：以上文献信息为示例，实际引用时需核实具体来源及准确性。如需真实文献，建议通过PubMed、Google Scholar等平台检索关键词(如“recombinant alpha-1 antitrypsin”)。
AAT1 (Alpha-1 Antitrypsin), also known as SERPINA1. is a glycoprotein primarily synthesized in the liver and plays a critical role in protecting tissues from damage caused by neutrophil-derived proteases, particularly neutrophil elastase. As a member of the serpin superfamily, it inhibits excessive protease activity through a unique "suicide substrate" mechanism. Genetic deficiency of AAT1. often caused by mutations like the Z variant (Glu342Lys), leads to insufficient protease inhibition, resulting in lung diseases such as emphysema and chronic obstructive pulmonary disease (COPD), as well as liver pathologies due to protein aggregation.
Recombinant AAT1 protein has emerged as a therapeutic and research tool to address AAT deficiency and explore its broader biological functions. Produced through genetic engineering in expression systems like mammalian cells (e.g., CHO cells) or yeast, recombinant AAT1 maintains the native protein's structure and function while ensuring scalability and purity. Its production involves optimizing codon usage, post-translational modifications (particularly glycosylation at three asparagine residues), and proper folding to preserve protease inhibition capacity.
Beyond replacement therapy for genetic AAT deficiency, recombinant AAT1 is investigated for its anti-inflammatory, immunomodulatory, and cytoprotective properties. Recent studies suggest potential applications in diabetes, autoimmune disorders, and even COVID-19. leveraging its ability to modulate cytokine release and protect endothelial cells. Additionally, it serves as a critical reagent for diagnostic assays, drug screening, and mechanistic studies of serpin biology. The development of modified recombinant variants with enhanced stability or extended half-life continues to expand its therapeutic potential while addressing challenges like short plasma persistence and production costs.
×
