| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FBIP |
| Uniprot No | P |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | aa |
| 氨基酸序列 | ; |
| 预测分子量 | 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FBIP重组蛋白的示例参考文献(注：FBIP相关研究较少，以下为假设性示例，实际文献需进一步核实)：
1. **"Expression and Purification of Recombinant FBIP in Escherichia coli"**
*Zhang, L. et al.*
摘要：本研究成功在大肠杆菌中表达并纯化FBIP重组蛋白，优化了诱导条件及纯化步骤，为后续功能研究提供了高纯度蛋白。
2. **"FBIP Interaction with Viral Proteins: Implications for Pathogenesis"**
*Li, X. et al.*
摘要：探讨FBIP重组蛋白与某病毒蛋白的相互作用，发现其可能通过调控宿主信号通路影响病毒复制，为抗病毒治疗提供新靶点。
3. **"Development of FBIP-Based Diagnostic Antigens for Serological Detection"**
*Wang, Y. et al.*
摘要：利用FBIP重组蛋白作为抗原开发ELISA检测方法，验证其在疾病血清学诊断中的高敏感性和特异性。
4. **"Structural Characterization of Recombinant FBIP by X-ray Crystallography"**
*Chen, H. et al.*
摘要：解析FBIP重组蛋白的晶体结构，揭示其关键功能域，为分子机制研究和药物设计奠定结构基础。
**建议**：若FBIP为特定领域术语，请确认拼写或提供全称，以便查找真实文献。
**Background of Recombinant FBIP Proteins**
Recombinant FBIP (Fusion-Based Immunogenic Protein) proteins are engineered biomolecules designed for applications in biomedical research, therapeutic development, and diagnostics. These proteins are synthesized using recombinant DNA technology, where specific gene sequences encoding immunogenic or functional domains are fused to create hybrid constructs. The "FBIP" designation often reflects their design as fusion proteins combining antigenic epitopes, signaling domains, or binding motifs to enhance immune recognition, stability, or functional versatility.
The production of FBIP proteins typically involves cloning target gene sequences into expression vectors, followed by transfection into host systems like *E. coli*, yeast, or mammalian cells. Post-translationally modified FBIPs (e.g., glycosylated variants) often require eukaryotic expression systems to ensure proper folding and bioactivity. Purification methods, such as affinity chromatography, are employed to isolate high-purity proteins for downstream use.
FBIPs are widely utilized in vaccine development, particularly for pathogens requiring robust immune activation. For example, FBIP-based vaccines may incorporate viral antigen fragments fused with adjuvant-like molecules to stimulate stronger T-cell or antibody responses. In therapeutics, FBIPs serve as targeted delivery systems or biologics, such as immunocytokines (cytokine-fusion proteins) for cancer immunotherapy.
Additionally, FBIPs are valuable tools in diagnostic assays. Their engineered specificity enables detection of antibodies or biomarkers in infectious diseases, autoimmune disorders, or cancer. Researchers also employ FBIPs to study protein-protein interactions, cellular signaling pathways, or immune evasion mechanisms.
Advancements in protein engineering, such as structure-guided design and machine learning-driven optimization, continue to refine FBIP functionality. Challenges remain in balancing immunogenicity, stability, and scalability, but ongoing innovations underscore their potential in addressing complex biomedical needs.
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