| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | p65 |
| Uniprot No | Q04206 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-210aa |
| 氨基酸序列 | MDELFPLIFPAEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGFYEAELCPDRCIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFQVPIEEQRGDYDLNAVRLCFQVTVRDPSGRPLRLPPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGD |
| 预测分子量 | 27.7 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p65重组蛋白的3篇参考文献示例(注：文献信息为虚构示例，仅用于演示格式)：
1. **文献名称**：*Expression and Purification of Recombinant p65 for NF-κB Signaling Studies*
**作者**：Smith A, et al.
**摘要**：该研究描述了一种利用大肠杆菌表达系统高效表达和纯化重组p65蛋白的方法，并通过凝胶迁移实验(EMSA)验证其与DNA结合活性，为NF-κB通路体外研究提供工具。
2. **文献名称**：*Structural Analysis of Recombinant p65 in Complex with IκBα*
**作者**：Lee C, et al.
**摘要**：通过X射线晶体学解析重组p65蛋白与抑制蛋白IκBα的复合物结构，揭示了两者相互作用的分子机制，为设计NF-κB抑制剂奠定基础。
3. **文献名称**：*Recombinant p65 as a Tool for Screening Anti-inflammatory Compounds*
**作者**：Wang Y, et al.
**摘要**：利用重组p65蛋白建立高通量筛选平台，鉴定出多种抑制p65核转位的小分子化合物，为治疗炎症性疾病提供潜在药物候选。
4. **文献名称**：*Functional Characterization of Phosphorylation Sites on Recombinant p65*
**作者**：Garcia R, et al.
**摘要**：通过体外激酶实验和质谱分析，鉴定重组p65蛋白的关键磷酸化位点，并证明其修饰对NF-κB转录活性的调控作用。
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如需真实文献，建议在PubMed或Google Scholar中搜索关键词 **"recombinant p65 protein"** 或 **"NF-kB p65 purification"**。
**Background of p65 Recombinant Protein**
The p65 protein, also known as RelA, is a critical subunit of the nuclear factor-kappa B (NF-κB) transcription factor family, which regulates genes involved in immune responses, inflammation, cell survival, and proliferation. Structurally, p65 contains a conserved N-terminal Rel homology domain (RHD) responsible for DNA binding, dimerization, and interaction with inhibitory proteins (IκBs), as well as a C-terminal transactivation domain (TAD) that recruits coactivators to initiate transcription.
In canonical NF-κB signaling, p65 forms heterodimers with p50. Under resting conditions, these dimers are sequestered in the cytoplasm by IκBs. Pro-inflammatory stimuli, such as TNF-α or IL-1β, activate the IκB kinase (IKK) complex, leading to IκB phosphorylation and degradation. This releases p65/p50 dimers, enabling their nuclear translocation and binding to κB motifs in target gene promoters, including cytokines, chemokines, and anti-apoptotic factors. Dysregulation of p65 is linked to chronic inflammation, autoimmune diseases, and cancer.
Recombinant p65 protein is engineered using expression systems like *E. coli* or mammalian cells, often tagged with affinity markers (e.g., His or GST) for purification. It serves as a vital tool for studying NF-κB pathways, screening inhibitors, and elucidating mechanisms of diseases like rheumatoid arthritis or lymphoma. Additionally, p65 recombinant proteins are used in *in vitro* binding assays, structural studies, and developing therapeutic strategies targeting NF-κB hyperactivity. Its application extends to reporter gene assays, where p65 activity is monitored to assess signaling dynamics or drug efficacy.
Overall, p65 recombinant protein is indispensable for advancing research in immunology, oncology, and drug discovery, offering insights into cellular responses and therapeutic interventions.
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