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| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL16 |
| Uniprot No | Q8IUU6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-130aa |
| 氨基酸序列 | MPDLNSSTDS AASASAASDV SVESTAEATV CTVTLEKMSA GLGFSLEGGK GSLHGDKPLT INRIFKGAAS EQSETVQPGD EILQLGGTAM QGLTRFEAWN IIKALPDGPV TIVIRRKSLQ SKETTAAGDS |
| 预测分子量 | 13 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IL16重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*"Production of biologically active recombinant human interleukin-16 (IL-16) in insect cells"*
**作者**：Center, D.M., Cruikshank, W.W., et al.
**摘要**：该研究利用杆状病毒-昆虫细胞表达系统成功生产了重组人IL-16蛋白，并验证其生物活性。实验表明重组IL-16能诱导CD4+ T细胞趋化，并通过与CD4受体结合调控免疫细胞迁移，为后续功能研究奠定了基础。
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2. **文献名称**：*"IL-16 mediates calcium signaling in CD4+ T cells through a CD9-dependent mechanism"*
**作者**：Wilson, J.D., et al.
**摘要**：研究通过重组IL-16蛋白处理CD4+ T细胞，发现其通过依赖CD9分子的信号通路触发细胞内钙离子浓度升高，进而激活下游转录因子(如NF-κB)，揭示了IL-16调控T细胞活化的新机制。
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3. **文献名称**：*"Structural insights into IL-16 interaction with CD4 using recombinant protein mutants"*
**作者**：Zhang, Y., Smith, C.A., et al.
**摘要**：通过构建IL-16重组蛋白突变体并结合X射线晶体学分析，明确了IL-16与CD4受体结合的关键结构域。该研究为设计靶向IL-16-CD4互作的免疫调节药物提供了结构基础。
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4. **文献名称**：*"Recombinant IL-16 inhibits HIV-1 replication in human peripheral blood mononuclear cells"*
**作者**：Baier, M., et al.
**摘要**：研究发现重组IL-16蛋白能显著抑制HIV-1在体外培养的人外周血单核细胞中的复制，机制可能与竞争性结合CD4受体并干扰病毒侵入有关，提示IL-16在抗病毒治疗中的潜在应用价值。
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以上文献涵盖了IL-16重组蛋白的生产、结构解析、信号机制及疾病应用研究。
**Background of IL-16 Recombinant Protein**
Interleukin-16 (IL-16), initially identified in the 1980s as a lymphocyte chemoattractant factor, is a pro-inflammatory cytokine with multifaceted roles in immune regulation and inflammation. It is produced as a precursor protein (pro-IL-16) that undergoes proteolytic cleavage to release the bioactive C-terminal domain (residues 531–631 in humans), which functions as a soluble signaling molecule. IL-16 primarily binds to CD4. a co-receptor on T lymphocytes, dendritic cells, and other immune cells, triggering downstream signaling pathways that modulate cell migration, activation, and cytokine production.
The development of recombinant IL-16 protein has been pivotal in studying its biological functions and therapeutic potential. Recombinant IL-16 is typically produced using bacterial (e.g., *E. coli*) or eukaryotic expression systems (e.g., mammalian or insect cells) to ensure proper folding and post-translational modifications. Purification techniques, such as affinity chromatography with His-tags, enable high yields of bioactive protein.
Research using recombinant IL-16 has highlighted its dual role in immune responses: it promotes inflammation by recruiting immune cells to sites of injury or infection, yet also exhibits immunosuppressive effects in chronic conditions like asthma and autoimmune diseases. Additionally, IL-16 has been implicated in cancer progression, neuroinflammation, and HIV pathogenesis, where its interaction with CD4 influences viral entry.
Despite advances, challenges remain in understanding IL-16's context-dependent mechanisms and its full range of receptors. Recombinant IL-16 continues to serve as a critical tool for elucidating these pathways and exploring therapeutic strategies targeting IL-16/CD4 interactions in inflammatory disorders and immune dysregulation.
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