| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SERPINI1 |
| Uniprot No | Q99574 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 17-410aa |
| 氨基酸序列 | TGATFPEEAIADLSVNMYNRLRATGEDENILFSPLSIALAMGMMELGAQG STQKEIRHSMGYDSLKNGEEFSFLKEFSNMVTAKESQYVMKIANSLFVQN GFHVNEEFLQMMKKYFNAAVNHVDFSQNVAVANYINKWVENNTNNLVKDL VSPRDFDAATYLALINAVYFKGNWKSQFRPENTRTFSFTKDDESEVQIPM MYQQGEFYYGEFSDGSNEAGGIYQVLEIPYEGDEISMMLVLSRQEVPLAT LEPLVKAQLVEEWANSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIF IKDANLTGLSDNKEIFLSKAIHKSFLEVNEEGSEAAAVSGMIAISRMAVL YPQVIVDHPFFFLIRNRRTGTILFMGRVMHPETMNTSGHDFEEL |
| 预测分子量 | 45 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SERPINI1重组蛋白的3篇参考文献，包含文献名称、作者及摘要内容的简要概括：
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1. **文献名称**: *"SERPINI1 modulates tau phosphorylation and neuroprotection in Alzheimer’s disease"*
**作者**: Smith A, et al.
**摘要**: 研究揭示了SERPINI1重组蛋白通过抑制丝氨酸蛋白酶活性，调节Tau蛋白过度磷酸化，减少神经元凋亡，可能在阿尔茨海默病的神经保护中起关键作用。
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2. **文献名称**: *"Recombinant SERPINI1 inhibits tumor invasion by suppressing urokinase-type plasminogen activator (uPA)"*
**作者**: Chen L, et al.
**摘要**: 通过体外实验证明，SERPINI1重组蛋白能够有效抑制uPA介导的细胞外基质降解，降低癌细胞侵袭能力，为癌症治疗提供了潜在靶点。
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3. **文献名称**: *"Structural and functional characterization of SERPINI1 recombinant protein in neuroserpinopathies"*
**作者**: González G, et al.
**摘要**: 利用X射线晶体学解析了SERPINI1重组蛋白的三维结构，发现其突变体(如G392E)因错误折叠导致聚合体沉积，与家族性脑部疾病的病理机制相关。
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**备注**：以上文献信息为模拟示例，实际文献需通过PubMed、Google Scholar等平台检索确认。如需具体文献，建议使用关键词“SERPINI1 recombinant protein”或结合研究领域(如神经退行性疾病、癌症)进一步筛选。
SERPINI1. also known as neuroserpin, is a member of the serine protease inhibitor (serpin) superfamily, primarily expressed in the central and peripheral nervous systems. It plays a critical role in regulating proteolytic activity by inhibiting tissue plasminogen activator (tPA) and plasmin, enzymes involved in fibrinolysis, synaptic plasticity, and neuronal survival. Neuroserpin’s dysfunction is linked to neurodegenerative disorders, such as familial encephalopathy with neuroserpin inclusion bodies (FENIB), characterized by intracellular protein aggregation due to mutations in the SERPINI1 gene.
Recombinant SERPINI1 protein is produced using expression systems like *E. coli* or mammalian cell lines to mimic its native structure and function. This engineered protein retains the conserved serpin domain, including the reactive center loop (RCL) responsible for protease binding and inhibition. Researchers often modify it with tags (e.g., His-tag) for purification or tracking. Its stability and activity are optimized for *in vitro* studies, enabling investigations into neuroserpin’s inhibitory mechanisms, interactions with proteases, and pathological aggregation pathways.
Studies leveraging recombinant SERPINI1 have advanced understanding of its neuroprotective roles, such as modulating extracellular matrix remodeling during brain development and mitigating neuronal damage post-injury. It also serves as a tool for drug screening targeting serpinopathies or thrombolytic therapies. Additionally, recombinant neuroserpin is explored as a potential therapeutic agent for stroke or Alzheimer’s disease, where excessive protease activity contributes to neurodegeneration. Its production in controlled systems ensures reproducibility for both basic research and clinical applications, bridging insights into serpin biology and therapeutic innovation.
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