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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL12B |
| 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 | IWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSG KTLTIQVKEFGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKE PKNKTFLRCEAKNYSGRFTCWWLTTISTDLTFSVKSSRGSSDPQGVTCGA ATLSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAVHKLKYEN YTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLT FCVQVQGKSKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEW ASVPCS |
| 预测分子量 | 35 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IL12B重组蛋白的模拟参考文献示例(仅供参考，非真实文献)：
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1. **《Expression and Purification of Recombinant IL12B in Escherichia coli》**
*作者：Smith A, et al.*
**摘要**：本研究报道了在大肠杆菌系统中高效表达重组IL12B蛋白的优化方法，通过密码子优化和包涵体复性策略获得可溶性蛋白，并验证其与IL12A亚基的结合能力，为后续功能研究奠定基础。
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2. **《Structural Analysis of IL12B Reveals Key Domains for Cytokine Receptor Interaction》**
*作者：Chen L, et al.*
**摘要**：通过X射线晶体学解析重组IL12B的三维结构，发现其N端结构域对IL-12受体β1亚基的结合至关重要，为设计靶向IL-12信号通路的药物提供结构基础。
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3. **《IL12B Recombinant Protein Enhances Antitumor Immunity in Murine Models》**
*作者：Wang Y, et al.*
**摘要**：在小鼠黑色素瘤模型中，局部注射重组IL12B联合IL12A显著激活NK细胞和Th1免疫应答，抑制肿瘤生长并延长生存期，提示其作为免疫佐剂的潜力。
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4. **《Functional Characterization of IL12B in Chronic Inflammatory Diseases》**
*作者：Kim J, et al.*
**摘要**：体外实验表明，重组IL12B单独处理可诱导单核细胞分泌IFN-γ，并协同IL-23加重银屑病样炎症反应，揭示其在自身免疫疾病中的双重调控作用。
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**注**：以上文献为基于学术常识构建的示例，实际研究中请通过PubMed、Web of Science等平台检索真实文献。
**Background of IL12B Recombinant Protein**
Interleukin-12B (IL12B), a key subunit of the heterodimeric cytokine IL-12. plays a pivotal role in bridging innate and adaptive immunity. IL-12 consists of two subunits, IL12A (p35) and IL12B (p40), which are encoded by separate genes and linked via disulfide bonds to form the bioactive p70 protein. IL12B, the p40 subunit, is essential for IL-12's stability and receptor binding, primarily activating natural killer (NK) and T cells to produce interferon-gamma (IFN-γ), thereby driving Th1-mediated immune responses against intracellular pathogens and tumors.
Recombinant IL12B is produced using biotechnological platforms, such as mammalian (e.g., CHO cells) or prokaryotic expression systems, followed by purification to ensure high specificity and low endotoxin levels. Its production enables research and therapeutic exploration, particularly in oncology and infectious diseases. IL-12 has shown potential in cancer immunotherapy by enhancing cytotoxic T-cell activity and suppressing angiogenesis. However, systemic toxicity limited its early clinical use, prompting strategies like localized delivery or combination with checkpoint inhibitors to improve safety.
Beyond IL-12. the IL12B subunit also pairs with IL-23A (p19) to form IL-23. another cytokine involved in chronic inflammation and autoimmune disorders. This duality underscores IL12B's functional versatility and complicates its therapeutic targeting. Recombinant IL12B proteins are critical tools for dissecting these pathways, developing biologics (e.g., anti-IL12/IL-23 antibodies), and optimizing vaccine adjuvants.
In summary, IL12B recombinant protein serves as a cornerstone for understanding Th1 immunobiology and advancing immunotherapies, balancing its therapeutic promise with mechanistic complexity.
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