首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | IL-12 |
Uniprot No | P43432 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 23-335aa |
氨基酸序列 | MWELEKDVYVVEVDWTPDAPGETVNLTCDTPEEDDITWTSDQRHGVIGSG KTLTITVKEFLDAGQYTCHKGGETLSHSHLLLHKKENGIWSTEILKNFKN KTFLKCEAPNYSGRFTCSWLVQRNMDLKFNIKSSSSSPDSRAVTCGMASL SAEKVTLDQRDYEKYSVSCQEDVTCPTAEETLPIELALEARQQNKYENYS TSFFIRDIIKPDPPKNLQMKPLKNSQVEVSWEYPDSWSTPHSYFSLKFFV RIQRKKEKMKETEEGCNQKGAFLVEKTSTEVQCKGGNVCVQAQDRYYNSS CSKWACVPCRVRS |
预测分子量 | 36 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-12重组蛋白的示例参考文献(注:以下信息为模拟示例,非真实文献,实际文献需通过数据库查询):
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1. **文献名称**:*Recombinant IL-12 enhances antitumor immunity by promoting T cell and NK cell activation*
**作者**:Smith et al., 2010
**摘要**:研究证明重组IL-12通过激活CD8+ T细胞和自然杀伤(NK)细胞,显著抑制小鼠肿瘤模型的生长,并延长生存期。其机制与IFN-γ分泌增加及肿瘤血管正常化相关。
2. **文献名称**:*IL-12 as a vaccine adjuvant: Synergistic effects in adaptive immune responses*
**作者**:Zhang et al., 2015
**摘要**:重组IL-12作为疫苗佐剂可增强抗原特异性T细胞和抗体反应,尤其在病毒和肿瘤疫苗中表现出协同效应,但需注意剂量依赖性毒性问题。
3. **文献名称**:*Targeted delivery of IL-12 via nanoparticle systems reduces systemic toxicity in cancer therapy*
**作者**:Wang et al., 2018
**摘要**:开发了一种基于纳米颗粒的IL-12递送系统,可在肿瘤微环境中局部释放IL-12.减少全身性副作用(如细胞因子风暴),同时提高抗肿瘤疗效。
4. **文献名称**:*IL-12 in autoimmune disease: Dual roles and therapeutic potential*
**作者**:Lee et al., 2020
**摘要**:探讨IL-12在自身免疫性疾病中的双重作用,指出其重组蛋白在特定条件下可调节Th1/Th2平衡,但过量可能加剧炎症,需精准调控应用。
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建议通过PubMed、Google Scholar等平台检索真实文献,关键词如“recombinant IL-12”、“IL-12 immunotherapy”。
Interleukin-12 (IL-12) is a heterodimeric cytokine composed of p35 (IL-12α) and p40 (IL-12β) subunits, primarily produced by antigen-presenting cells such as dendritic cells and macrophages. Discovered in the early 1990s, IL-12 plays a pivotal role in bridging innate and adaptive immunity by promoting Th1 cell differentiation, enhancing cytotoxic T and NK cell activity, and stimulating interferon-gamma (IFN-γ) production. Its receptor, expressed on T and NK cells, activates JAK-STAT signaling pathways, particularly STAT4. driving pro-inflammatory responses critical for combating intracellular pathogens and tumors.
Recombinant IL-12 (rIL-12) is produced using genetic engineering techniques, typically in mammalian or bacterial expression systems. Early clinical interest focused on its anticancer potential due to its ability to enhance antitumor immunity. However, systemic toxicity in early-phase trials (e.g., dose-dependent immunopathologies) limited therapeutic application. This led to refined strategies, including localized delivery (intratumoral, inhaled) and combination therapies with checkpoint inhibitors or adoptive cell therapies.
In infectious diseases, rIL-12 has shown promise in preclinical models for leishmaniasis, tuberculosis, and viral infections by bolstering pathogen-specific Th1 responses. It also serves as a vaccine adjuvant to improve cellular immunity. Recent advances in protein engineering aim to optimize its pharmacokinetics and reduce toxicity through structural modifications or fusion proteins.
Despite challenges, IL-12 remains a key immunomodulator under investigation in over 100 clinical trials, with renewed interest in controlled-release formulations and gene therapy approaches. Its dual role in immune activation and regulation continues to inspire therapeutic innovations across oncology, infectious diseases, and immunotherapy.
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