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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL12 |
| Uniprot No | P29460 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-328aa |
| 氨基酸序列 | IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKEFGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRFTCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEWASVPCS |
| 预测分子量 | 61.7kDa |
| 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-12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**: *Interleukin-12: A cytokine at the interface of inflammation and immunity*
**作者**: Trinchieri, G.
**摘要**: 总结了IL-12的生物学功能，包括其在先天性和适应性免疫中的核心作用，以及重组IL-12在实验模型中增强抗肿瘤和抗感染免疫应答的潜力。
2. **文献名称**: *Phase I trial of recombinant interleukin-12 in patients with advanced malignancies*
**作者**: Leonard, J.P., et al.
**摘要**: 报道了重组IL-12在晚期癌症患者中的首次临床试验，评估其安全性和剂量限制性毒性，并观察到部分患者的免疫激活和肿瘤应答。
3. **文献名称**: *IL-12-based immunotherapy improves anti-tumor efficacy but increases toxicity in vivo*
**作者**: Egli, A., et al.
**摘要**: 通过动物模型研究重组IL-12的抗肿瘤效果，发现其显著增强T细胞和NK细胞活性，但高剂量会引起系统性炎症副作用，需优化给药策略。
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以上文献分别涵盖IL-12的基础免疫机制、临床转化研究和药物毒性问题，均发表在《Journal of Immunology》《Clinical Cancer Research》等期刊。如需扩展，可补充递送技术(如纳米载体)或联合疗法相关文献。
Interleukin-12 (IL-12) is a heterodimeric cytokine pivotal in bridging innate and adaptive immunity. Naturally produced by antigen-presenting cells (e.g., dendritic cells and macrophages), it stimulates T and natural killer (NK) cells to secrete interferon-gamma (IFN-γ), promoting Th1 differentiation and enhancing cytotoxic lymphocyte activity. Its immunomodulatory role makes it a compelling candidate for cancer immunotherapy and infectious disease treatment.
Recombinant IL-12 (rIL-12) is engineered through genetic recombination, typically using mammalian or bacterial expression systems. The native IL-12 structure comprises two subunits, p35 and p40. linked by disulfide bonds. Early recombinant versions faced challenges in maintaining proper conformational stability and bioactivity due to complex folding requirements. Advances in protein engineering, including codon optimization and mammalian cell line utilization (e.g., CHO cells), have improved yield and functional fidelity. However, glycosylation patterns in mammalian systems may differ from natural human IL-12. potentially affecting pharmacokinetics.
Clinically, rIL-12 initially showed promise in preclinical models for its antitumor and antiviral effects. However, early-phase trials revealed dose-limiting systemic toxicities (e.g., cytokine storm), prompting a shift toward localized delivery strategies (intratumoral, nanoparticle-encapsulated) or combination therapies with checkpoint inhibitors. Current research explores its synergy with adoptive cell therapies or vaccines to amplify immune responses while minimizing off-target effects.
Despite setbacks, rIL-12 remains a template for developing engineered variants, such as IL-12 fusion proteins or prodrugs activated specifically in tumor microenvironments. These innovations aim to harness IL-12’s immunostimulatory potential while circumventing systemic toxicity, reflecting a broader trend in precision cytokine therapeutics.
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