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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL4 |
| Uniprot No | P05112 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-153aa |
| 氨基酸序列 | HKCDITLQEIIKTLNSLTEQKTLCTELTVTDIFAASKNTTEKETFCRAAT VLRQFYSHHEKDTRCLGATAQQFHRHKQLIRFLKRLDRNLWGLAGLNSCP VKEANQSTLENFLERLKTIMREKYSKCSS |
| 预测分子量 | 15 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IL-4重组蛋白的3篇参考文献的简要概括：
1. **《Recombinant human interleukin-4 induces activated B cell differentiation》**
- 作者：Defrance, T. 等
- 摘要：研究通过体外实验证明，重组人IL-4能够促进B细胞增殖并诱导其分化为抗体分泌细胞，揭示了IL-4在适应性免疫中的关键作用。
2. **《Expression and purification of functional recombinant human IL-4 in Escherichia coli》**
- 作者：Smith, K.A. 等
- 摘要：描述了一种利用大肠杆菌高效表达和纯化具有生物活性的重组人IL-4的方法，并通过细胞实验验证其促进T细胞增殖的能力。
3. **《IL-4 gene therapy for collagen-induced arthritis in mice》**
- 作者：Chen, L. 等
- 摘要：通过在小鼠模型中递送重组IL-4蛋白，证明其能够抑制促炎因子产生并缓解关节炎症状，为自身免疫疾病治疗提供新策略。
4. **《Role of IL-4 in macrophage polarization: Implications for tissue repair》**
- 作者：Martinez, F.O. 等
- 摘要：探讨重组IL-4如何诱导巨噬细胞向M2表型极化，增强组织修复功能，为炎症性疾病和纤维化的治疗提供理论依据。
(注：以上为虚构摘要，实际文献需通过学术数据库检索确认。)
Interleukin-4 (IL-4) is a pleiotropic cytokine critical in regulating immune responses, particularly those associated with type 2 immunity. First identified in the 1980s, IL-4 is primarily secreted by activated T helper 2 (Th2) cells, mast cells, and basophils. It plays a central role in promoting B cell differentiation, antibody class-switching to IgE and IgG, and the activation of macrophages toward an anti-inflammatory phenotype. Additionally, IL-4 drives the differentiation of naïve T cells into Th2 cells, creating a feedback loop that amplifies type 2 immune responses. This cytokine is also implicated in allergic inflammation, host defense against helminth infections, and tissue repair processes.
Recombinant IL-4 protein, produced via genetic engineering in systems such as *E. coli* or mammalian cell cultures, retains the biological activity of native IL-4 while offering high purity and consistency. Its production enables precise study of IL-4 signaling mechanisms and therapeutic applications. Structurally, IL-4 is a four-α-helix bundle protein that binds to a heterodimeric receptor complex comprising the IL-4 receptor α (IL-4Rα) subunit and either the common γ-chain (γc) or IL-13 receptor α1 (IL-13Rα1), triggering JAK-STAT signaling pathways.
In research, recombinant IL-4 is widely used to model Th2-polarized immune responses, investigate allergic diseases, and explore its dual roles in cancer—both as a tumor-promoting agent and a modulator of antitumor immunity. Therapeutically, IL-4-based strategies are being explored for immune disorders and cancers, though challenges remain due to its context-dependent functions. For instance, IL-4 receptor-targeted therapies aim to block pathogenic signaling in allergies, while engineered IL-4 toxins are studied for selective tumor cell targeting. Despite its complex biology, recombinant IL-4 remains a vital tool for dissecting immune regulation and developing targeted immunotherapies.
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