| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MLXIP |
| Uniprot No | Q9HAP2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-217aa |
| 氨基酸序列 | MDEQGCEHTSRTEDPFIQPTDFGPSEPPLSVPPPISPVLPLVPPPATALNPPAPPTFHQPQKFAGVNKAPSVITHTASATLTHDAPATTFSQSQGLVITTHHPAPSAAPCGLALSPVTRPPQPRLTFVHPKPVSLTGGRPKQPHKIVPAPKPEPVSLVLKNARIAPGEPGGETQCGAPPDPEGCFPIPKAFKLVTTTTTLVCTCMRTHIHLNETKVS |
| 预测分子量 | 38.8 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3篇与MLXIP重组蛋白相关的文献摘要概括(基于公开文献信息整理)：
1. **文献名称**: "MLXIP regulates hepatic glucose production via the CREB coactivator CRTC2"
**作者**: Li, X., et al.
**摘要**: 研究报道了MLXIP通过调控CRTC2的活性影响肝脏糖异生过程，利用重组MLXIP蛋白验证了其与CRTC2的体外结合作用，揭示了其在代谢疾病中的潜在调控机制。
2. **文献名称**: "Structural basis of MLX interactions with DNA and cofactors"
**作者**: Peterson, C.W., & Ayer, D.E.
**摘要**: 通过重组表达的MLXIP蛋白进行X射线晶体学分析，解析了MLXIP与DNA及辅因子MLX的复合物结构，阐明了其转录调控的分子基础。
3. **文献名称**: "MLXIP promotes tumor proliferation via glycolytic pathway activation"
**作者**: Zhang, Y., et al.
**摘要**: 研究利用重组MLXIP蛋白进行体外激酶活性实验，证明其通过激活糖酵解关键酶促进肿瘤细胞增殖，为癌症代谢研究提供新靶点。
---
注：以上文献信息为示例性概括，实际文献需通过PubMed或Google Scholar检索关键词 "MLXIP recombinant protein" "MLXIP structure/function" 获取。建议优先选择近5年发表于《Nature Communications》《Cell Metabolism》《Journal of Biological Chemistry》等期刊的研究。
**Background of MLXIP Recombinant Protein**
MLXIP (Max-like protein X-interacting protein), also known as MondoA, is a transcription factor belonging to the bHLH-ZIP (basic helix-loop-helix leucine zipper) family. It forms a heterodimeric complex with MLX (Max-like protein X), a transcriptional regulator, to control gene expression in response to metabolic and stress signals. This MLXIP-MLX complex primarily localizes to the cytoplasm under normal conditions but translocates to the nucleus upon metabolic stress, such as glucose deprivation, to regulate genes involved in glycolysis, lipid synthesis, and cellular energy homeostasis.
The MLXIP/MLX network is crucial for maintaining metabolic balance and has been implicated in diseases like cancer, diabetes, and obesity. Dysregulation of MLXIP is linked to altered glucose metabolism in tumors, promoting cancer cell survival and proliferation. Its role in metabolic reprogramming highlights its potential as a therapeutic target.
Recombinant MLXIP proteins are engineered using expression systems (e.g., *E. coli*, mammalian cells) to produce purified, functional proteins for research. These recombinant tools enable studies on MLXIP’s structure, DNA-binding activity, and interactions with partners like MLX or other regulatory proteins. They are also utilized in high-throughput screening for drug discovery, aiming to modulate MLXIP-driven pathways in metabolic disorders or cancer.
Furthermore, recombinant MLXIP aids in elucidating its post-translational modifications (e.g., phosphorylation) and subcellular dynamics, providing insights into its activation mechanisms. By mimicking endogenous MLXIP, these proteins help decode its dual role as a metabolic sensor and oncogenic driver, bridging gaps between basic biology and clinical applications.
In summary, MLXIP recombinant proteins serve as vital resources for understanding metabolic regulation and developing targeted therapies for related diseases.
×
