| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NFKBID |
| Uniprot No | Q8NI38 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-313aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMEAGPWRVSAPPSGPPQFPAVVPGPSL EVARAHMLALGPQQLLAQDEEGDTLLHLFAARGLRWAAYAAAEVLQVYRR LDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAAT YGLPGVLLAVLNSGVQVDLEARDFEGLTPLHTAILALNVAMRPSDLCPRV LSTQARDRLDCVHMLLQMGANHTSQEIKSNKTVLHLAVQAANPTLVQLLL ELPRGDLRTFVNMKAHGNTALHMAAALPPGPAQEAIVRHLLAAGADPTLR NLENEQPVHLLRPGPGPEGLRQLLKRSRVAPPGLSS |
| 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NFKBID重组蛋白的3篇参考文献示例(注：以下为虚构文献，仅用于示例格式，实际文献需通过学术数据库查询)：
1. **文献名称**：*"NFKBID regulates canonical NF-κB signaling through its interaction with p65"*
**作者**：Smith J, et al.
**摘要**：研究揭示了重组NFKBID蛋白通过结合NF-κB亚基p65抑制其核转位，在炎症反应中起负调控作用，并验证了其在体外模型中的功能。
2. **文献名称**：*"Structural characterization of recombinant NFKBID and its role in T-cell activation"*
**作者**：Zhang Y, et al.
**摘要**：通过原核系统表达并纯化NFKBID重组蛋白，解析其晶体结构，发现其C端结构域对T细胞受体信号通路的抑制作用至关重要。
3. **文献名称**：*"NFKBID deficiency promotes B-cell lymphoma development via dysregulated NF-κB pathways"*
**作者**：Lee C, et al.
**摘要**：利用重组NFKBID蛋白进行功能补偿实验，证明其缺失导致B细胞中非经典NF-κB通路过度激活，与淋巴瘤发生相关。
如需真实文献，建议在PubMed或Google Scholar中以关键词“NFKBID recombinant protein”或“IκBL/NFKBID function”检索。
NFκBID (Nuclear Factor Kappa B Inhibitor Delta), also known as IκBD, is a member of the IκB protein family that regulates the activity of NF-κB transcription factors. NF-κB plays a central role in immune responses, inflammation, cell survival, and proliferation by controlling the expression of genes involved in these processes. Under basal conditions, IκB proteins, including NFκBID, bind to NF-κB dimers in the cytoplasm, masking their nuclear localization signals and sequestering them in an inactive state. Upon stimulation by cytokines, pathogens, or stress signals, IκB proteins are phosphorylated and degraded via the ubiquitin-proteasome pathway, allowing NF-κB to translocate into the nucleus and activate target genes.
NFκBID is unique among IκB proteins due to its atypical structure and regulatory mechanisms. Unlike canonical IκBα or IκBβ, NFκBID lacks the C-terminal PEST domain involved in protein stability but contains ankyrin repeats critical for NF-κB binding. Its expression is tightly regulated and often induced by NF-κB itself, forming a feedback loop to modulate signaling duration and intensity.
Recombinant NFκBID proteins are engineered in vitro using expression systems like E. coli or mammalian cells, enabling functional and structural studies. These purified proteins are essential tools for investigating NFκBID's interactions with NF-κB subunits (e.g., p50. p65), its degradation dynamics, and its role in diseases such as cancer, autoimmune disorders, or chronic inflammation. Researchers also utilize recombinant NFκBID to screen therapeutic compounds targeting NF-κB hyperactivation. Understanding its molecular mechanisms may lead to novel strategies for fine-tuning NF-κB signaling in pathological conditions.
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