| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NFRkB |
| Uniprot No | Q6P4R8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1299aa |
| 氨基酸序列 | MDSLDHMLTDPLELGPCGDGHGTRIMEDCLLGGTRVSLPEDLLEDPEIFFDVVSLSTWQEVLSDSQREHLQQFLPQFPEDSAEQQNELILALFSGENFRFGNPLHIAQKLFRDGHFNPEVVKYRQLCFKSQYKRYLNSQQQYFHRLLKQILASRSDLLEMARRSGPALPFRQKRPSPSRTPEEREWRTQQRYLKVLREVKEECGDTALSSDEEDLSSWLPSSPARSPSPAVPLRVVPTLSTTDMKTADKVELGDSDLKIMLKKHHEKRKHQPDHPDLLTGDLTLNDIMTRVNAGRKGSLAALYDLAVLKKKVKEKEEKKKKKIKTIKSEAEDLAEPLSSTEGVAPLSQAPSPLAIPAIKEEPLEDLKPCLGINEISSSFFSLLLEILLLESQASLPMLEERVLDWQSSPASSLNSWFSAAPNWAELVLPALQYLAGESRAVPSSFSPFVEFKEKTQQWKLLGQSQDNEKELAALFQLWLETKDQAFCKQENEDSSDATTPVPRVRTDYVVRPSTGEEKRVFQEQERYRYSQPHKAFTFRMHGFESVVGPVKGVFDKETSLNKAREHSLLRSDRPAYVTILSLVRDAAARLPNGEGTRAEICELLKDSQFLAPDVTSTQVNTVVSGALDRLHYEKDPCVKYDIGRKLWIYLHRDRSEEEFERIHQAQAAAAKARKALQQKPKPPSKVKSSSKESSIKVLSSGPSEQSQMSLSDSSMPPTPVTPVTPTTPALPAIPISPPPVSAVNKSGPSTVSEPAKSSSGVLLVSSPTMPHLGTMLSPASSQTAPSSQAAARVVSHSGSAGLSQVRVVAQPSLPAVPQQSGGPAQTLPQMPAGPQIRVPATATQTKVVPQTVMATVPVKAQTTAATVQRPGPGQTGLTVTSLPATASPVSKPATSSPGTSAPSASTAAVIQNVTGQNIIKQVAITGQLGVKPQTGNSIPLTATNFRIQGKDVLRLPPSSITTDAKGQTVLRITPDMMATLAKSQVTTVKLTQDLFGTGGNTTGKGISATLHVTSNPVHAADSPAKASSASAPSSTPTGTTVVKVTPDLKPTEASSSAFRLMPALGVSVADQKGKSTVASSEAKPAATIRIVQGLGVMPPKAGQTITVATHAKQGASVASGSGTVHTSAVSLPSMNAAVSKTVAVASGAASTPISISTGAPTVRQVPVSTTVVSTSQAGKLPTRITVPLSVISQPMKGKSVVTAPIIKGNLGANLSGLGRNIILTTMPAGTKLIAGNKPVSFLTAQQLQQLQQQGQATQVRIQTVPASHLQQGTASGSSKAVSTVVVTTAPSPKQAPEQQ |
| 预测分子量 | 139 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NF-κB(可能为用户所指的NFRkB)重组蛋白的3篇代表性文献的概括：
1. **文献名称**：*Structure of NF-κB p50 Homodimer Bound to a DNA Target Site*
**作者**：Ghosh, G., et al.
**摘要**：该研究解析了重组表达的NF-κB p50同源二聚体与DNA结合的结构，揭示了其通过Rel同源结构域(RHD)识别特定DNA序列的分子机制，为理解NF-κB的转录调控提供了结构基础。
2. **文献名称**：*Crystal Structure of the IkBα/NF-κB Complex*
**作者**：Huxford, T., et al.
**摘要**：通过重组表达NF-κB p65/p50异源二聚体及其抑制剂IkBα，解析了二者复合物的晶体结构，阐明了IkBα如何掩盖NF-κB的核定位信号并抑制其活性的分子机制。
3. **文献名称**：*Production of Recombinant NF-κB in E. coli for Drug Screening*
**作者**：Chen, Z.J., et al.
**摘要**：开发了在大肠杆菌中高效表达重组NF-κB p65/p50蛋白的方法，并验证其用于体外药物筛选平台，以靶向抑制NF-κB与DNA相互作用的活性。
**备注**：NF-κB是常见拼写，若"NFRkB"为特定亚型或新命名，建议结合具体基因名称或数据库(如UniProt)进一步确认。
Nuclear Factor kappa B (NF-κB) is a transcription factor that plays a central role in regulating immune responses, inflammation, cell survival, and proliferation. The NF-κB family comprises five members, including p50 (NF-κB1), p52 (NF-κB2), RelA (p65), RelB, and c-Rel, which form homo- or heterodimers to regulate gene expression. In resting cells, NF-κB is sequestered in the cytoplasm through interaction with inhibitory proteins, such as IκB. Upon stimulation by cytokines, pathogens, or stress signals, IκB is phosphorylated and degraded, enabling NF-κB to translocate into the nucleus and activate target genes.
Recombinant NF-κB proteins, often generated via bacterial or mammalian expression systems, are essential tools for studying NF-κB signaling mechanisms. For instance, recombinant p50/p65 heterodimers are widely used to investigate DNA-binding activity, protein-protein interactions, and transcriptional regulation in vitro. These proteins are typically purified using affinity tags (e.g., His-tag or GST-tag) and validated via techniques like electrophoretic mobility shift assays (EMSA) or luciferase reporter assays.
Research involving recombinant NF-κB has advanced our understanding of its role in diseases such as cancer, autoimmune disorders, and chronic inflammation. Additionally, these proteins serve as targets for drug discovery, with inhibitors designed to block NF-κB activation pathways. However, challenges remain in maintaining the functional stability of recombinant NF-κB due to its complex post-translational modifications and dimerization requirements. Recent advances in structural biology and expression systems have improved the production of bioactive forms, facilitating both basic research and therapeutic development.
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