| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SAP |
| Uniprot No | O60880-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-128aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MDAVAVYHGK ISRETGEKLL LATGLDGSYL LRDSESVPGV YCLCVLYHGY IYTYRVSQTE TGSWSAETAP GVHKRYFRKI KNLISAFQKP DQGIVIPLQY PVEKKSSARS TQGTTGIRED PDVCLKAP |
| 预测分子量 | 16 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SAP(血清淀粉样蛋白P成分)重组蛋白的3篇参考文献，按研究主题分类简要概括：
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1. **文献名称**：*"Recombinant Human Serum Amyloid P Component: Production, Purification, and Structural Characterization"*
**作者**：Smith A. et al.
**摘要**：研究报道了通过哺乳动物表达系统高效生产重组人SAP蛋白的方法，优化了纯化工艺，并通过质谱和X射线晶体学验证了其与天然SAP一致的结构和糖基化修饰特征。
2. **文献名称**：*"Targeting SAP in Alzheimer's Disease: Recombinant SAP Antibodies Reduce Amyloid-β Plaque Burden in Mouse Models"*
**作者**：Chen L. et al.
**摘要**：探讨重组SAP蛋白在阿尔茨海默病淀粉样斑块形成中的作用，开发靶向SAP的单克隆抗体，并在小鼠模型中证明其可减少淀粉样沉积并改善认知功能。
3. **文献名称**：*"Recombinant SAP as a Potential Anti-fibrotic Therapy: Attenuation of Liver Fibrosis in Experimental Models"*
**作者**：Wang Y. et al.
**摘要**：研究发现重组SAP蛋白通过调节巨噬细胞极化和TGF-β信号通路，显著减轻小鼠肝纤维化模型中的胶原沉积，提示其作为抗纤维化治疗药物的潜力。
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**备注**：以上文献为示例性概括，实际文献需通过PubMed或Web of Science以关键词“recombinant serum amyloid P component”检索获取近年研究。如需具体文献，建议补充研究领域(如疾病机制、药物开发等)以进一步筛选。
**Background of Recombinant SAP Protein**
Serum Amyloid P component (SAP) is a naturally occurring plasma protein belonging to the pentraxin family, characterized by its pentameric structure and calcium-dependent ligand-binding properties. It plays roles in innate immunity, inflammation regulation, and tissue homeostasis by interacting with apoptotic cells, microbial pathogens, and extracellular matrix components. SAP is also implicated in amyloidosis, where it stabilizes pathologic amyloid fibrils, contributing to disease progression.
Recombinant SAP (rSAP) is produced using genetic engineering techniques, typically expressed in prokaryotic (e.g., *E. coli*) or eukaryotic (e.g., mammalian cell) systems. Its recombinant form retains the functional properties of native SAP, enabling controlled studies without reliance on human plasma extraction. This has accelerated research into SAP's biological mechanisms and therapeutic potential. For instance, rSAP is explored as a diagnostic or therapeutic target in amyloidosis, fibrosis, and autoimmune diseases. In Alzheimer’s disease, SAP's interaction with amyloid-β has spurred interest in developing inhibitors to block fibril deposition.
Challenges in rSAP production include ensuring proper post-translational modifications (e.g., glycosylation) critical for functionality, often necessitating eukaryotic expression systems. Advances in protein engineering, such as site-specific mutagenesis, have improved yield and stability. Additionally, rSAP serves as a tool to study SAP's role in modulating immune responses, including its anti-inflammatory effects via Fcγ receptor interactions.
Overall, recombinant SAP provides a versatile platform for both basic research and clinical applications, offering insights into amyloid-related disorders and inflammation while paving the way for novel biologics. Its development underscores the importance of recombinant technologies in bridging mechanistic understanding and therapeutic innovation.
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