纯度 | >98 % SDS-PAGE. |
种属 | Human |
靶点 | BRD2 |
Uniprot No | P25440 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 65-187aa |
氨基酸序列 | EVSNPKKPGRVTNQLQYLHKVVMKALWKHQFAWPFRQPVDAVKLGLPDYH KIIKQPMDMGTIKRRLENNYYWAASECMQDFNTMFTNCYIYNKPTDDIVL MAQTLEKIFLQKVASMPQEEQEL |
预测分子量 | 16 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BRD2重组蛋白的3篇参考文献,涵盖结构解析、功能研究及药物开发方向:
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1. **文献名称**:*Selective inhibition of BET bromodomains*
**作者**:Filippakopoulos, P. et al.
**摘要**:该研究解析了BRD2等BET蛋白的溴结构域晶体结构,利用重组BRD2蛋白验证了小分子抑制剂JQ1的结合模式,揭示了其通过竞争性结合抑制转录的机制,为靶向表观遗传调控提供依据(Nature, 2010)。
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2. **文献名称**:*Inhibition of BET recruitment to chromatin as an effective treatment for MLL-fusion leukaemia*
**作者**:Dawson, M.A. et al.
**摘要**:研究通过重组BRD2蛋白进行体外结合实验,证明BET抑制剂可阻断BRD2与组蛋白乙酰化位点互作,抑制白血病细胞增殖,为BRD2在癌症治疗中的应用提供实验支持(Nature, 2011)。
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3. **文献名称**:*Suppression of inflammation by a synthetic histone mimic*
**作者**:Nicodeme, E. et al.
**摘要**:利用重组BRD2蛋白进行高通量筛选,发现小分子I-BET可靶向BRD2溴结构域,抑制炎症相关基因表达,阐明了BRD2在免疫调控中的功能及药物开发潜力(Nature Chemical Biology, 2010)。
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这些文献分别从结构生物学、疾病机制及药物筛选角度,展示了重组BRD2蛋白在基础研究与转化医学中的关键作用。
BRD2 (Bromodomain-containing protein 2) is a member of the bromodomain and extra-terminal (BET) family of epigenetic regulators, which play critical roles in chromatin remodeling and transcriptional regulation. It contains two tandem bromodomains that specifically recognize acetylated lysine residues on histone tails, enabling its interaction with acetylated chromatin. BRD2 is involved in cell cycle progression, inflammation, and oncogenesis, with dysregulation linked to cancers, autoimmune disorders, and neurological conditions.
Recombinant BRD2 proteins are engineered in vitro using expression systems like *E. coli* or mammalian cells to produce functional domains, particularly the bromodomains, for biochemical and structural studies. These purified proteins retain the ability to bind acetylated histones and small-molecule inhibitors, making them essential tools for drug discovery. For example, BRD2 recombinant proteins are widely used in high-throughput screening to identify BET inhibitors, which have therapeutic potential for cancer and inflammatory diseases.
Structural studies using recombinant BRD2. often in complex with ligands or chromatin partners, have revealed key binding mechanisms and conformational changes. This has guided the design of selective inhibitors to target BET proteins while minimizing off-target effects. Additionally, BRD2 recombinant variants with mutations in critical residues (e.g., asparagine mutations in the acetyl-lysine binding pocket) serve as controls to validate drug specificity.
The availability of recombinant BRD2 accelerates research into BET protein biology and supports the development of epigenetic therapies. Its applications span X-ray crystallography, NMR, biophysical assays, and cellular studies, bridging molecular insights with translational drug development.
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