| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MED24 |
| Uniprot No | O75448 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-989aa |
| 活性数据 | MKVVNLKQAILQAWKERWSDYQWAINMKKFFPKGATWDILNLADALLEQAMIGPSPNPLILSYLKYAISSQMVSYSSVLTAISKFDDFSRDLCVQALLDIMDMFCDRLSCHGKAEECIGLCRALLSALHWLLRCTAASAERLREGLEAGTPAAGEKQLAMCLQRLEKTLSSTKNRALLHIAKLEEASSWTAIEHSLLKLGEILANLSNPQLRSQAEQCGTLIRSIPTMLSVHAEQMHKTGFPTVHAVILLEGTMNLTGETQSLVEQLTMVKRMQHIPTPLFVLEIWKACFVGLIESPEGTEELKWTAFTFLKIPQVLVKLKKYSHGDKDFTEDVNCAFEFLLKLTPLLDKADQRCNCDCTNFLLQECGKQGLLSEASVNNLMAKRKADREHAPQQKSGENANIQPNIQLILRAEPTVTNILKTMDADHSKSPEGLLGVLGHMLSGKSLDLLLAAAAATGKLKSFARKFINLNEFTTYGSEESTKPASVRALLFDISFLMLCHVAQTYGSEVILSESRTGAEVPFFETWMQTCMPEEGKILNPDHPCFRPDSTKVESLVALLNNSSEMKLVQMKWHEACLSISAAILEILNAWENGVLAFESIQKITDNIKGKVCSLAVCAVAWLVAHVRMLGLDEREKSLQMIRQLAGPLFSENTLQFYNERVVIMNSILERMCADVLQQTATQIKFPSTGVDTMPYWNLLPPKRPIKEVLTDIFAKVLEKGWVDSRSIHIFDTLLHMGGVYWFCNNLIKELLKETRKEHTLRAVELLYSIFCLDMQQVTLVLLGHILPGLLTDSSKWHSLMDPPGTALAKLAVWCALSSYSSHKGQASTRQKKRHREDIEDYISLFPLDDVQPSKLMRLLSSNEDDANILSSPTDRSMSSSLSASQLHTVNMRDPLNRVLANLFLLISSILGSRTAGPHTQFVQWFMEECVDCLEQGGRGSVLQFMPFTTVSELVKVSAMSSPKVVLAITDLSLPLGRQVAAKAIAAL |
| 分子量 | 136.7 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人MED24蛋白的3条参考文献示例(注：文献标题与作者为虚构示例，仅供格式参考)：
1. **文献名称**：Structural Insights into Human MED24 and Its Role in Transcriptional Regulation
**作者**：Zhang L, et al.
**摘要**：本研究通过X射线晶体学解析了重组人MED24蛋白的核心结构，揭示了其与中介体复合物其他亚基的相互作用界面，并发现MED24通过构象变化调控RNA聚合酶II的募集。
2. **文献名称**：MED24 Acts as a Coactivator in Nuclear Receptor Signaling Pathways
**作者**：Thompson R, et al.
**摘要**：文章利用重组MED24蛋白进行体外结合实验，证明其与维生素D受体(VDR)和甲状腺激素受体(TR)直接互作，调控靶基因转录，提示MED24在核激素信号通路中的关键辅助激活功能。
3. **文献名称**：Dysregulation of MED24 in Cancer: Implications for Cell Proliferation
**作者**：Wang Y, et al.
**摘要**：通过分析乳腺癌细胞系，研究发现重组人MED24蛋白的异常表达可通过激活Myc转录程序促进细胞增殖，为MED24作为癌症治疗靶点提供了实验依据。
如需真实文献，建议通过PubMed或Google Scholar以“MED24 protein structure/function/recombinant”为关键词检索。
MED24. a subunit of the Mediator complex, plays a critical role in transcriptional regulation by bridging transcription factors and RNA polymerase II. The human Mediator complex, comprising ~30 subunits, acts as a universal adaptor that integrates diverse cellular signals to modulate gene expression. MED24. also known as vitamin D receptor-interacting protein (DRIP24/ARC100), is part of the Mediator’s middle module, which stabilizes interactions between transcription activators and the basal transcription machinery. Structurally, MED24 contains conserved domains, including KIX and SPXX motifs, enabling interactions with transcription factors like CREB, p53. and nuclear receptors.
Studies highlight MED24’s involvement in pathways regulating cell cycle progression, differentiation, and metabolic responses. Dysregulation of MED24 is linked to cancers, neurological disorders, and metabolic diseases. For example, its overexpression in prostate cancer correlates with androgen receptor signaling, while mutations affect neural development. Recombinant human MED24 protein, produced via bacterial or mammalian expression systems, is essential for dissecting Mediator complex assembly and gene regulatory mechanisms. It is purified using affinity tags (e.g., His or GST tags) and validated for functional assays, such as protein-protein interaction studies, in vitro transcription, and chromatin binding experiments. Researchers utilize recombinant MED24 to explore therapeutic targeting of transcriptional dysregulation, offering insights into precision medicine approaches for diseases driven by aberrant Mediator function. Its applications span structural biology, drug screening, and mechanistic studies of transcriptional enhancers/suppressors.
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