| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NFkB |
| Uniprot No | Q9Y6Q6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-202aa |
| 氨基酸序列 | LQIAPPCTSEKHYEHLGRCCNKCEPGKYMSSKCTTTSDSVCLPCGPDEYLDSWNEEDKCLLHKVCDTGKALVAVVAGNSTTPRRCACTAGYHWSQDCECCRRNTECAPGLGAQHPLQLNKDTVCKPCLAGYFSDAFSSTDKCRPWTNCTFLGKRVEHHGTEKSDAVCSSSLPARK |
| 预测分子量 | 23.2 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3条关于NF-κB重组蛋白研究的参考文献示例(内容为虚构，仅用于格式演示)：
1. **"Recombinant NF-κB p50/p65 heterodimer: Structural insights into DNA binding specificity"**
*作者：Smith J, et al.*
摘要：通过大肠杆菌表达系统纯化重组NF-κB p50/p65异源二聚体，结合X射线晶体学分析其与DNA结合的构象变化，揭示了关键氨基酸残基在靶基因识别中的作用。
2. **"Functional characterization of a truncated recombinant IκBα protein for inflammation modulation"**
*作者：Lee H, et al.*
摘要：构建并表达截短型IκBα重组蛋白，证明其可通过竞争性抑制NF-κB与DNA结合，降低巨噬细胞中炎症因子TNF-α和IL-6的表达水平。
3. **"High-yield production of active NF-κB in insect cells: Application in drug screening assays"**
*作者：Wang Y, et al.*
摘要：利用杆状病毒-昆虫细胞系统规模化制备功能性NF-κB重组蛋白，并建立基于荧光素酶报告基因的化合物筛选平台，用于鉴定NF-κB抑制剂。
4. **"Dynamic interaction between recombinant RelA and IKKγ revealed by single-molecule imaging"**
*作者：Garcia R, et al.*
摘要：通过单分子FRET技术分析重组RelA蛋白与IKKγ的实时相互作用，阐明IKK复合物激活NF-κB的动力学机制。
(注：以上文献为模拟示例，实际研究需查询真实数据库如PubMed或Web of Science。)
Nuclear factor kappa B (NFκB) is a family of transcription factors central to immune responses, inflammation, cell survival, and proliferation. Discovered in 1986. NFκB regulates genes involved in cytokines, chemokines, adhesion molecules, and stress responses. Inactive NFκB resides in the cytoplasm, bound to inhibitory proteins (IκBs). Signaling via Toll-like receptors, cytokines, or stress activates the IκB kinase (IKK) complex, leading to IκB phosphorylation, ubiquitination, and proteasomal degradation. This liberates NFκB dimers (e.g., p50/p65) to translocate into the nucleus and initiate target gene transcription.
Recombinant NFκB proteins are engineered for research and therapeutic applications. They are typically produced in bacterial (e.g., E. coli) or mammalian expression systems. Common forms include full-length subunits (p65. p50), truncated versions (e.g., p50 lacking the transactivation domain), or fusion proteins tagged with markers like GST or His for purification. Structural studies often utilize the Rel homology domain (RHD), which mediates DNA binding and dimerization.
Recombinant NFκB enables in vitro analysis of DNA-binding activity (e.g., EMSA), protein interactions (co-IP, pull-down assays), and structural characterization (X-ray crystallography). It’s also used to screen inhibitors targeting NFκB activation pathways, such as IKK inhibitors. In cell-based assays, recombinant proteins help dissect signaling dynamics or rescue NFκB-deficient models. Therapeutic exploration includes engineered dominant-negative mutants to suppress pathological NFκB activity in chronic inflammation or cancer.
Challenges include maintaining proper folding and post-translational modifications (e.g., phosphorylation), often requiring mammalian expression systems. Despite this, recombinant NFκB remains indispensable for decoding its regulatory mechanisms and developing targeted therapies.
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