| 纯度 | >97%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SAA |
| Uniprot No | P0DJI8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-122aa |
| 氨基酸序列 | RSFFSFLGEA FDGARDMWRA YSDMREANYI GSDKYFHARG NYDAAKRGPG GVWAAEAISD ARENIQRFFG HGAEDSLADQ AANEWGRSGK DPNHFRPAGL PEKY |
| 预测分子量 | 11.7 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SAA重组蛋白的3篇代表性文献的简要信息(注：文献为模拟示例，非真实存在)：
1. **文献名称**: *"High-yield Expression and Purification of Recombinant Human Serum Amyloid A (SAA1) in Escherichia coli"*
**作者**: Smith, J.R. et al.
**摘要**: 本研究报道了一种利用大肠杆菌表达系统高效表达人源SAA1重组蛋白的方法，并通过亲和层析和凝胶过滤技术实现高纯度蛋白制备。实验验证了重组SAA1的二级结构与天然蛋白相似，且在体外炎症模型中可激活巨噬细胞NF-κB通路。
2. **文献名称**: *"Functional Characterization of Recombinant SAA in Acute-phase Immune Responses"*
**作者**: Chen, L. & Wang, H.
**摘要**: 通过重组SAA蛋白研究其在急性期反应中的免疫调节作用，发现SAA可通过结合TLR2/4受体促进促炎细胞因子(如IL-6、TNF-α)分泌，并揭示了其介导胆固醇代谢调控的分子机制。
3. **文献名称**: *"Recombinant SAA Aggregation Dynamics and Its Role in Amyloidosis"*
**作者**: Müller, T. et al.
**摘要**: 利用重组SAA蛋白探究淀粉样纤维形成机制，发现pH和金属离子浓度显著影响其聚集动力学，研究为淀粉样变性疾病的病理机制及药物靶点开发提供了实验依据。
如需真实文献，建议在PubMed或Web of Science中检索关键词：**"recombinant serum amyloid A"**或**"SAA protein expression"**。近年研究多聚焦于SAA在炎症、代谢疾病及癌症中的功能与应用。
Serum Amyloid A (SAA) is a family of apolipoproteins predominantly produced by the liver in response to inflammatory cytokines during acute-phase reactions. As a key biomarker of inflammation, SAA levels rise rapidly in infections, tissue injury, or chronic diseases. Native SAA exists in multiple isoforms, with SAA1 and SAA2 being major acute-phase proteins, while SAA4 is constitutively expressed.
Recombinant SAA proteins are engineered using genetic cloning techniques to express specific isoforms in heterologous systems like *E. coli* or mammalian cells. This approach overcomes limitations of purifying SAA from natural sources, which is challenging due to low abundance, structural heterogeneity, and contamination risks. Recombinant technology ensures high purity, consistency, and scalability, making it vital for research and therapeutic applications.
The production typically involves inserting the SAA gene into expression vectors, followed by protein extraction, refolding (if expressed as inclusion bodies), and purification via chromatography. Recombinant SAA retains functional properties, including binding to Toll-like receptors (TLRs) and high-density lipoprotein (HDL), enabling studies on its roles in inflammation, immune regulation, and lipid metabolism.
Applications span disease mechanism studies (e.g., amyloidosis, atherosclerosis), drug discovery targeting SAA-mediated pathways, and diagnostic kit development. Additionally, recombinant SAA serves as a tool to investigate its dual role in host defense and pathological processes, such as promoting pro-inflammatory cytokine release or tissue repair. Despite progress, challenges remain in mimicking post-translational modifications and isoform-specific functions, driving ongoing optimization of expression systems. Recombinant SAA continues to advance both basic research and clinical solutions in inflammatory and metabolic disorders.
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