| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IkBe |
| Uniprot No | O00221 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-500aa |
| 氨基酸序列 | MNQRRSESRP GNHRLQAYAE PGKGDSGGAG PLSGSARRGR GGGGAIRVRR PCWSGGAGRG GGPAWAVRLP TVTAGWTWPA LRTLSSLRAG PSEPHSPGRR PPRAGRPLCQ ADPQPGKAAR RSLEPDPAQT GPRPARAAGM SEARKGPDEA EESQYDSGIE SLRSLRSLPE STSAPASGPS DGSPQPCTHP PGPVKEPQEK EDADGERADS TYGSSSLTYT LSLLGGPEAE DPAPRLPLPH VGALSPQQLE ALTYISEDGD TLVHLAVIHE APAVLLCCLA LLPQEVLDIQ NNLYQTALHL AVHLDQPGAV RALVLKGASR ALQDRHGDTA LHVACQRQHL ACARCLLEGR PEPGRGTSHS LDLQLQNWQG LACLHIATLQ KNQPLMELLL RNGADIDVQE GTSGKTALHL AVETQERGLV QFLLQAGAQV DARMLNGCTP LHLAAGRGLM GISSTLCKAG ADSLLRNVED ETPQDLTEES LVLLPFDDLK ISGKLLLCTD |
| 预测分子量 | 52,8 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IκBα重组蛋白的3篇参考文献示例(注：文献信息为模拟概括，具体引用时请核实原文)：
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1. **文献名称**: *Purification and Functional Analysis of Recombinant IκBα Expressed in E. coli*
**作者**: Smith J, et al.
**摘要**: 该研究报道了在大肠杆菌中高效表达并纯化重组人IκBα蛋白的方法，通过体外实验证实其可有效抑制NF-κB与DNA的结合活性，为信号通路研究提供工具。
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2. **文献名称**: *Structural Insights into IκBα-NF-κB Interaction by X-ray Crystallography*
**作者**: Huxford T, et al.
**摘要**: 利用重组IκBα蛋白解析了其与NF-κB复合物的晶体结构，揭示了IκBα通过锚蛋白重复结构域结合NF-κB p65亚基的分子机制。
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3. **文献名称**: *IκBα Phosphorylation Mutants as Dominant-Negative Inhibitors of NF-κB Signaling*
**作者**: Malek S, et al.
**摘要**: 构建了IκBα磷酸化位点突变的重组蛋白，证明其在细胞中可阻断内源性IκBα降解，显著抑制炎症因子诱导的NF-κB激活。
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**备注**：实际研究中建议通过PubMed或Web of Science以关键词“recombinant IκBα protein”“IκBα purification”等检索最新文献，并优先选择高影响力期刊(如*Nature*、*Cell*或*JBC*)的论文。
IkBe (IκB epsilon) is a member of the inhibitor of κB (IκB) family, which plays a critical role in regulating the NF-κB signaling pathway. NF-κB, a transcription factor involved in immune responses, inflammation, and cell survival, is typically sequestered in the cytoplasm by binding to IκB proteins. Upon stimulation by cytokines, pathogens, or stress signals, IκB proteins undergo phosphorylation and ubiquitination, leading to their proteasomal degradation. This releases NF-κB, allowing it to translocate to the nucleus and activate target genes.
IkBe, encoded by the NFKBIE gene, shares structural homology with other IκB proteins, including ankyrin repeats that mediate interactions with NF-κB dimers. Unlike the prototypical IκBα, IkBe exhibits distinct regulatory features, such as preferential binding to specific NF-κB complexes (e.g., p50/c-Rel) and tissue-specific expression, particularly in immune cells. Its expression is dynamically regulated by NF-κB itself, forming a feedback loop to modulate signaling duration and intensity. Dysregulation of IkBe has been implicated in chronic inflammation, autoimmune diseases, and cancers, highlighting its therapeutic potential.
Recombinant IkBe proteins are engineered for research and therapeutic applications. Produced via bacterial or mammalian expression systems, these proteins retain functional domains required for NF-κB interaction. Purification techniques like affinity chromatography (e.g., His-tag) ensure high purity. Recombinant IkBe is widely used in mechanistic studies to dissect NF-κB activation dynamics, screen small-molecule inhibitors, or develop biologics targeting aberrant NF-κB activity. It also serves as a tool in assays such as EMSA, ChIP, or luciferase reporter systems to quantify NF-κB inhibition. Despite lacking post-translational modifications in prokaryotic systems, recombinant IkBe remains valuable for in vitro and cell-based studies, offering insights into inflammatory pathways and drug discovery.
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