纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | SerpinA5 |
Uniprot No | P05154 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 20-406aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMHRHHPREMKKRVEDLHVGATVAPSSRRDF TFDLYRALASAAPSQNIFFSPVSISMSLAMLSLGAGSSTKMQILEGLGLN LQKSSEKELHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDLQDTFVSA MKTLYLADTFPTNFRDSAGAMKQINDYVAKQTKGKIVDLLKNLDSNAVVI MVNYIFFKAKWETSFNHKGTQEQDFYVTSETVVRVPMMSREDQYHYLLDR NLSCRVVGVPYQGNATALFILPSEGKMQQVENGLSEKTLRKWLKMFKKRQ LELYLPKFSIEGSYQLEKVLPSLGISNVFTSHADLSGISNHSNIQVSEMV HKAVVEVDESGTRAAAATGTIFTFRSARLNSQRLVFNRPFLMFIVDNNIL FLGKVNRP |
预测分子量 | 46 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SerpinA5重组蛋白的3篇代表性文献(示例参考格式,内容为虚构示例):
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1. **文献名称**: *Recombinant SerpinA5 inhibits tumor cell invasion by modulating urokinase plasminogen activator activity*
**作者**: Smith J, et al.
**摘要**: 研究报道了重组SerpinA5蛋白通过抑制尿激酶型纤溶酶原激活物(uPA)的活性,降低肿瘤细胞外基质降解能力,从而抑制乳腺癌细胞侵袭的分子机制。
2. **文献名称**: *Expression and purification of biologically active human SerpinA5 in Escherichia coli*
**作者**: Lee H, et al.
**摘要**: 描述了利用大肠杆菌表达系统高效制备重组SerpinA5蛋白的优化方法,并通过质谱和功能实验验证其抑制凝血酶和纤溶酶的生物活性。
3. **文献名称**: *SerpinA5 deficiency exacerbates inflammation in sepsis models: Rescue by recombinant protein administration*
**作者**: Zhang R, et al.
**摘要**: 通过动物实验证明,外源性重组SerpinA5蛋白可减轻脓毒症模型中的过度炎症反应,其机制与抑制中性粒细胞弹性蛋白酶活性相关。
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*注:以上文献为示例性内容,实际引用需以真实发表的论文为准。建议通过PubMed或Google Scholar搜索关键词“SerpinA5 recombinant”或“Protein C inhibitor expression”获取具体文献。*
SerpinA5. also known as protein C inhibitor (PCI), is a member of the serine protease inhibitor (serpin) superfamily. It plays a regulatory role in multiple biological processes, including blood coagulation, fibrinolysis, inflammation, and cellular homeostasis. Structurally, SerpinA5 contains a conserved reactive center loop (RCL) that interacts with target proteases, forming irreversible complexes to inhibit their enzymatic activity. It is expressed in various tissues, including the liver, reproductive organs, and endothelial cells, and is encoded by the SERPINA5 gene located on chromosome 14 in humans.
Recombinant SerpinA5 protein is produced using biotechnological methods, such as expression in bacterial (e.g., *E. coli*) or mammalian cell systems, to ensure proper folding and post-translational modifications. This engineered protein retains the functional properties of native SerpinA5. enabling researchers to study its interactions with proteases like activated protein C (APC), thrombin, and urokinase-type plasminogen activator (uPA). Its anticoagulant and antifibrinolytic roles are of particular interest in thrombosis and hemostasis research. Additionally, SerpinA5 has been implicated in pathological conditions, including cancer metastasis, inflammatory diseases, and reproductive disorders, making its recombinant form a valuable tool for mechanistic studies and therapeutic development.
Recent studies highlight its potential as a biomarker or therapeutic target, particularly in cancers where protease dysregulation drives invasion. The recombinant protein is often purified via affinity tags (e.g., His-tag) and validated for activity through protease inhibition assays. Ongoing research aims to clarify its tissue-specific functions and explore clinical applications in precision medicine.
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