| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CRP |
| Uniprot No | P02741 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-224aa |
| 氨基酸序列 | GQTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFYTELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGSEILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKSLKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVNMWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFTKPQLWP |
| 预测分子量 | 29.1 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. |
以下是模拟生成的关于CRP重组蛋白的参考文献示例(非真实文献，仅供格式参考)：
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1. **《High-yield expression and purification of human C-reactive protein in Escherichia coli》**
*作者：Zhang L, et al.*
摘要：研究通过优化大肠杆菌表达系统，实现了人源CRP重组蛋白的高效表达(产量达50 mg/L)，并建立两步层析纯化法，获得高纯度(>95%)蛋白。该蛋白在体外实验中显示出与天然CRP相似的磷酸胆碱结合活性。
2. **《CRP-based biosensors: Recombinant CRP as a biomarker detection tool in cardiovascular diseases》**
*作者：Kim S, Wang H.*
摘要：开发了一种基于CRP重组蛋白的免疫传感器，利用其与抗体的特异性结合特性，实现血清中CRP的快速定量检测(灵敏度0.1 μg/mL)，为心血管疾病诊断提供便携式解决方案。
3. **《Structural analysis of recombinant CRP mutants reveals key functional domains》****
*作者：Patel R, et al.*
摘要：通过构建CRP重组蛋白的突变体(如Ala取代Pentraxin结构域关键位点)，结合X射线晶体学分析，揭示了CRP与补体C1q结合的分子机制，为靶向CRP的抗炎药物设计提供依据。
4. **《Recombinant CRP as a potential therapeutic agent in sepsis: In vivo murine model study》**
*作者：Gupta A, et al.*
摘要：在脓毒症小鼠模型中，外源性重组CRP(10 mg/kg)显示出调节巨噬细胞炎症因子分泌的作用，低剂量可缓解过度炎症反应，提示其剂量依赖性治疗潜力。
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建议通过**PubMed/Google Scholar**检索真实文献，关键词：`recombinant C-reactive protein expression, purification, application`。部分真实研究机构(如剑桥大学、中科院)近年有相关论文发表。
C-reactive protein (CRP) is a highly conserved acute-phase protein synthesized primarily by hepatocytes in response to pro-inflammatory cytokines, particularly interleukin-6 (IL-6). It serves as a key biomarker of systemic inflammation and infection, with circulating levels rising rapidly within hours of tissue injury or microbial invasion. Structurally, CRP is a pentameric protein belonging to the pentraxin family, characterized by five identical subunits non-covalently assembled in a radial symmetry. Each subunit contains a calcium-dependent ligand-binding site that recognizes phosphocholine residues on damaged cell membranes or microbial surfaces, enabling CRP to participate in innate immune responses by opsonizing pathogens and activating complement pathways.
Recombinant CRP (rCRP) is produced using genetic engineering techniques, often expressed in bacterial (e.g., *E. coli*) or mammalian cell systems. Bacterial expression yields non-glycosylated protein, while eukaryotic systems produce glycosylated forms closer to native human CRP. The development of rCRP has addressed limitations in sourcing purified natural CRP, which is challenging due to low baseline plasma concentrations and contamination risks. Researchers utilize rCRP to study inflammatory mechanisms, drug interactions, and diagnostic applications. Its standardized production ensures batch-to-batch consistency for experimental reproducibility.
Clinically, rCRP is employed in assay calibration to quantify inflammation levels in cardiovascular diseases, autoimmune disorders, and infections. Emerging studies explore its role in atherosclerosis progression and cancer-associated inflammation. However, debates persist about its causal role in pathologies versus being a secondary marker. The accessibility of rCRP has accelerated both basic research into pentraxin biology and translational efforts to develop therapeutic agents targeting CRP-mediated pathways. Ongoing work focuses on engineering CRP variants with modified functional properties for tailored biomedical applications.
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