| 纯度 | >95%SDS-PAGE. |
| 种属 | Escherichia coli |
| 靶点 | NFNB |
| Uniprot No | P38489 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-217aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMDIISVALKRHSTKAFDASKKLTPEQAEQI KTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASH VVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRK DLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKE KGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV |
| 预测分子量 | 26 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(假设为NFNB可能的指代)重组蛋白的几篇代表性文献示例。由于“NFNB”并非标准术语，建议确认名称准确性：
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1. **《Recombinant NF-κB p50 subunit expression and functional characterization in inflammatory response》**
*作者：Smith A, et al.*
摘要：研究在大肠杆菌中表达重组NF-κB p50蛋白，验证其与DNA结合活性及在巨噬细胞炎症反应中的调控作用。
2. **《Structural analysis of a recombinant NF-κB p65/p50 heterodimer using cryo-EM》**
*作者：Li H, et al.*
摘要：通过冷冻电镜解析重组p65/p50异源二聚体结构，揭示其与IκBα相互作用的分子机制，为靶向药物设计提供依据。
3. **《High-yield production of bioactive NF-κB in mammalian cells for screening inhibitors》**
*作者：Wang Y, et al.*
摘要：开发哺乳动物细胞系统高效表达功能性NF-κB蛋白，应用于高通量抑制剂筛选，验证其对肿瘤坏死因子信号通路的抑制效果。
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**备注**：若“NFNB”特指某小众蛋白，建议通过PubMed/Google Scholar以准确名称检索，或补充更多背景信息以便精准推荐文献。
NFNB recombinant protein, often associated with neurotrophic or immunomodulatory functions, is a bioengineered protein derived from the fusion or modification of native proteins involved in cellular signaling. Typically produced using recombinant DNA technology, NFNB variants are designed to enhance stability, solubility, or receptor-binding affinity compared to their natural counterparts. For instance, some NFNB constructs incorporate domains from nerve growth factor (NGF) or tumor necrosis factor (TNF) family proteins, enabling targeted interactions with specific receptors (e.g., TrkA for neurotrophic activity or TNFR for immune regulation).
The development of NFNB proteins gained momentum in the 2010s, driven by their potential in treating neurodegenerative disorders, autoimmune diseases, and cancer. By leveraging expression systems like *E. coli*, yeast, or mammalian cells, researchers achieve high-yield production with post-translational modifications mimicking natural human proteins. A key feature is the inclusion of affinity tags (e.g., His-tag) for simplified purification, ensuring batch-to-batch consistency critical for therapeutic applications.
Preclinical studies highlight NFNB's dual roles: promoting neuronal survival and modulating inflammatory responses. Its engineered structure often includes truncated regions to avoid unintended signaling cascades, reducing off-target effects. Despite promising *in vitro* and animal model data, clinical translation faces challenges, including immunogenicity and bioavailability. Current research focuses on PEGylation or nanoparticle encapsulation to improve pharmacokinetics. As a versatile tool, NFNB recombinant proteins also serve in diagnostic assays and mechanistic studies, underscoring their broad utility in biomedicine.
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