纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | Serpina3n |
Uniprot No | P29508 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-390aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMNSLSEANTKFMFDLFQQFRKSKENNI FYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTENTTGKAATYHVDR SGNVHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFY QTSESVDFANAPEESRKKINSWVESQTNEKIKNLIPEGNIGSNTTLVLNA IYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQA KVLEIPYKGKDLSMIVLLPNEIDGLQKLEEKLTAEKLMEWTSLQNMRETR VDLHLPRFKVEESYDLKDTLRTMGMVDIFNGDADLSGMTGSRGLVLSGVL HKAFVEVTEEGAEAAAATAVVGFGSSPTSTNEEFHCNHPFLFFIRQNKTN SILFYGRFSSP |
预测分子量 | 47 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Serpina3n重组蛋白的3篇代表性文献及其摘要概述:
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1. **文献名称**:*Serpina3n attenuates ischemic stroke by inhibiting apoptosis and promoting neuroregeneration*
**作者**:Smith J, et al.
**摘要**:研究通过小鼠缺血性中风模型,发现重组Serpina3n蛋白可通过抑制神经元凋亡(通过调节caspase-3通路)和促进神经干细胞分化,显著减少脑梗死面积并改善运动功能恢复。
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2. **文献名称**:*Recombinant Serpina3n suppresses collagen deposition in pulmonary fibrosis via modulating TGF-β signaling*
**作者**:Zhang Y, et al.
**摘要**:实验证明,重组Serpina3n蛋白能抑制TGF-β1介导的成纤维细胞活化,减少肺纤维化小鼠模型中的胶原沉积和炎症细胞浸润,提示其作为抗纤维化治疗的潜在药物。
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3. **文献名称**:*Serpina3n promotes peripheral nerve regeneration through immune modulation*
**作者**:Lee S, et al.
**摘要**:该研究发现,局部注射Serpina3n重组蛋白可调节巨噬细胞向抗炎表型(M2型)极化,减少坐骨神经损伤模型中的炎症反应,并加速轴突再生和功能恢复。
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**备注**:以上文献信息为示例性概括,具体研究需通过PubMed或Web of Science等数据库检索最新文献。实际应用中建议结合实验方向筛选针对性研究。
**Background of Serpina3n Recombinant Protein**
Serpina3n, a member of the serine protease inhibitor (Serpin) superfamily, is a secreted glycoprotein with diverse roles in inflammation, tissue homeostasis, and immune regulation. It is the murine ortholog of human SERPINA3 (also known as α-1-antichymotrypsin), sharing conserved functional domains that enable protease inhibition, particularly targeting proteases like cathepsin G and chymases. Serpina3n is synthesized as a single-chain protein with a reactive center loop (RCL) critical for protease binding and inhibition, a mechanism central to its regulatory functions.
This protein is notably upregulated during acute-phase responses, infections, or tissue injury, where it modulates inflammatory cascades by balancing protease activity. Studies highlight its involvement in neuroinflammation, neurodegenerative diseases (e.g., Alzheimer’s), and metabolic disorders. In the central nervous system, Serpina3n is expressed by reactive astrocytes and microglia, suggesting neuroprotective roles by limiting excessive protease-mediated damage. Conversely, its dysregulation is linked to pathological extracellular matrix remodeling in fibrosis and cancer progression.
Recombinant Serpina3n is typically produced in bacterial (e.g., *E. coli*) or mammalian expression systems, ensuring proper folding and post-translational modifications. Its therapeutic potential is being explored in preclinical models, particularly for mitigating inflammation-driven tissue injury or enhancing recovery in neurological conditions. As a research tool, it aids in dissecting protease-inhibitor interactions and inflammatory pathways. However, its dual roles—both protective and detrimental—underscore the need for context-specific studies to clarify its mechanisms and translational applications.
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