| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SERPINA1 |
| Uniprot No | P01009 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-418aa |
| 氨基酸序列 | EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNI FFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELL RTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDT EEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEV KDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATA IFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLK SVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGA MFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK |
| 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SERPINA1重组蛋白的3篇参考文献及其摘要概括：
1. **标题**：*Recombinant Alpha-1 Antitrypsin Production in a Human Cell Line: Optimization and Characterization*
**作者**：Brantly, M., et al.
**摘要**：该研究描述了在HEK293细胞中高效表达重组SERPINA1(α1-抗胰蛋白酶，AAT)的方法，通过优化培养条件及启动子设计提高蛋白产量，并验证其抑制中性粒细胞弹性蛋白酶的活性，证实其与天然AAT功能相似。
2. **标题**：*Therapeutic Efficacy of Recombinant SERPINA1 in Alpha-1 Antitrypsin Deficiency-Related Emphysema*
**作者**：Sandhaus, R.A., et al.
**摘要**：通过临床试验评估重组SERPINA1对AAT缺乏症患者的治疗效果，结果显示静脉注射重组蛋白可显著提升血清AAT水平并减缓肺功能下降，支持其作为替代疗法的潜力。
3. **标题**：*Structural Analysis of Recombinant Alpha-1 Antitrypsin Using Cryo-Electron Microscopy*
**作者**：Lomas, D.A., et al.
**摘要**：利用冷冻电镜解析重组SERPINA1的三维结构，揭示其活性中心构象及与蛋白酶结合的分子机制，为设计更稳定的突变体以抑制异常聚合提供理论依据。
(注：上述文献为示例性内容，实际引用需根据具体研究检索数据库如PubMed获取。)
SERPINA1. also known as alpha-1 antitrypsin (AAT), is a glycoprotein encoded by the SERPINA1 gene and belongs to the serine protease inhibitor (serpin) superfamily. Primarily synthesized in the liver, it plays a critical role in regulating proteolytic enzymes, particularly neutrophil elastase, to protect tissues from excessive degradation during inflammatory responses. AAT deficiency, caused by mutations in the SERPINA1 gene (e.g., the Z variant), leads to impaired protein secretion, resulting in both lung tissue destruction (emphysema) and liver damage due to intracellular polymer accumulation.
Recombinant SERPINA1 protein is produced using biotechnological platforms, such as bacterial, yeast, or mammalian cell expression systems, to mimic the structure and function of native human AAT. This engineered protein is purified to high homogeneity, ensuring biological activity comparable to its endogenous counterpart. Its applications span both research and therapeutic domains. In research, recombinant SERPINA1 serves as a tool to study protease-inhibitor interactions, inflammatory pathways, and disease mechanisms linked to AAT deficiency. Therapeutically, it is used in augmentation therapy to slow lung function decline in AAT-deficient patients. Additionally, recombinant variants are being explored for enhanced stability, reduced immunogenicity, or targeted delivery to improve clinical efficacy. Beyond genetic deficiency, its anti-inflammatory and immunomodulatory properties are under investigation for conditions like chronic obstructive pulmonary disease (COPD), cystic fibrosis, and autoimmune disorders. Ongoing studies also focus on optimizing production methods and developing novel formulations to broaden its therapeutic potential.
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