| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VIP |
| Uniprot No | P01282 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-169aa |
| 氨基酸序列 | MDTRNKAQLLVLLTLLSVLFSQTSAWPLYRAPSALRLGDRIPFEGANEPD QVSLKEDIDMLQNALAENDTPYYDVSRNARHADGVFTSDFSKLLGQLSAK KYLESLMGKRVSNISEDPVPVKRHSDAVFTDNYTRLRKQMAVKKYLNSIL NGKRSSEGESPDFPEELEK |
| 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VIP重组蛋白的3-4条参考文献示例(注：文献信息为模拟内容，实际引用需核实)：
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1. **文献名称**: "Recombinant VIP production in *E. coli* and its immunomodulatory effects *in vitro*"
**作者**: Delgado, M., et al.
**摘要**: 研究通过大肠杆菌表达系统成功制备重组血管活性肠肽(VIP)，并验证其体外免疫调节功能。实验表明重组VIP可抑制巨噬细胞释放促炎因子(如TNF-α、IL-6)，提示其潜在抗炎应用。
2. **文献名称**: "Engineering a stable VIP analogue for therapeutic applications in inflammatory diseases"
**作者**: Ganea, D., et al.
**摘要**: 报道了一种通过基因工程改造的VIP类似物，优化其稳定性以抵抗酶解。该重组蛋白在类风湿性关节炎小鼠模型中显著减轻炎症反应，为慢性炎症疾病治疗提供新策略。
3. **文献名称**: "Structural optimization of recombinant VIP enhances stability and *in vivo* half-life"
**作者**: Smith, J., et al.
**摘要**: 通过定点突变和聚乙二醇(PEG)修饰技术提高重组VIP的稳定性和半衰期。药代动力学实验显示，修饰后的蛋白在小鼠体内停留时间延长，且保留原有生物活性。
4. **文献名称**: "Anti-inflammatory effects of recombinant VIP in sepsis models and immune cell modulation"
**作者**: Tanaka, S., et al.
**摘要**: 在脓毒症动物模型中验证重组VIP的治疗效果。结果显示，重组VIP通过抑制NF-κB信号通路减少细胞因子风暴，并促进调节性T细胞分化，显著提高生存率。
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**建议**：实际研究中，可通过PubMed、Web of Science等数据库搜索关键词(如“recombinant VIP protein”、“VIP expression and purification”、“therapeutic applications of VIP”)获取最新文献，并优先选择高影响力期刊(如*Nature Biotechnology*、*Biomaterials*)或权威综述。
**Background of Recombinant VIP (Vasoactive Intestinal Peptide)**
Vasoactive Intestinal Peptide (VIP), a 28-amino acid neuropeptide, was first isolated from the porcine intestine in the 1970s. It belongs to the secretin-glucagon peptide family and functions as a neurotransmitter, immunomodulator, and vasodilator. VIP exerts its effects by binding to G protein-coupled receptors (VPAC1 and VPAC2), regulating cellular processes like cAMP signaling, ion transport, and cytokine production. Its roles span neuroprotection, inflammation control, smooth muscle relaxation, and circadian rhythm modulation.
Traditional VIP extraction from natural sources is inefficient due to low abundance and high costs. Recombinant DNA technology emerged as a solution, enabling scalable production of VIP in heterologous systems (e.g., *E. coli*, yeast, or mammalian cells*). Recombinant VIP (rVIP) retains bioactivity while offering higher purity and consistency. However, challenges persist, including proper folding, post-translational modifications (e.g., phosphorylation), and stability during purification.
Research on rVIP has expanded its therapeutic potential. Preclinical studies highlight its efficacy in models of autoimmune diseases (e.g., rheumatoid arthritis), neurodegenerative disorders (e.g., Alzheimer’s), and cancer. Its anti-inflammatory and cytoprotective properties make it a candidate for treating sepsis, lung injury, and diabetes. Additionally, rVIP-based drug delivery systems (e.g., nanoparticles) are being explored to enhance bioavailability and target-specific action.
Despite progress, clinical translation remains limited by short half-life, rapid degradation, and off-target effects. Current efforts focus on engineering stabilized analogs, hybrid peptides, or fusion proteins to improve pharmacokinetics. As a multifunctional peptide, rVIP continues to bridge gaps between neurobiology, immunology, and regenerative medicine, holding promise for next-generation biologics.
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