| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MLX |
| Uniprot No | Q9HAP2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-244 aa |
| 活性数据 | MTEPGASPEDPWVKVEYAYSDNSLDPGLFVESTRKGSVVSRANSIGSTSASSVPNTDDEDSDYHQEAYKESYKDRRRRAHTQAEQKRRDAIKRGYDDLQTIVPTCQQQDFSIGSQKLSKAIVLQKTIDYIQFLHKEKKKQEEEVSTLRKDVTALKIMKVNYEQIVKAHQDNPHEGEDQVSDQVKFNVFQGIMDSLFQSFNASISVASFQELSACVFSWIEEHCKPQTLREIVIGVLHQLKNQLY |
| 分子量 | 52.58 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3篇与重组人MLX蛋白相关的代表性文献(注：以下为示例性虚构文献，实际引用需根据真实论文调整)：
---
1. **文献名称**：*Crystal structure and functional analysis of MLX reveals DNA-binding specificity in Myc/Max transcriptional network*
**作者**：Thompson R, et al.
**摘要**：该研究解析了重组人MLX蛋白的晶体结构，揭示了其与DNA结合的特定基序，并通过体外实验证明MLX通过与Max蛋白异源二聚化调控靶基因转录，影响细胞增殖与代谢通路。
---
2. **文献名称**：*MLX interacts with ChREBP to regulate glucose-responsive gene expression in hepatocytes*
**作者**：Li Y, et al.
**摘要**：本文通过免疫共沉淀和重组蛋白互作实验，证明MLX与碳水化合物反应元件结合蛋白(ChREBP)形成功能复合物，协同调控肝细胞中糖代谢相关基因(如LPK、ACC)的表达，揭示其在代谢稳态中的作用。
---
3. **文献名称**：*A novel role of MLX in suppressing tumorigenesis through competition with MYC for Max dimerization*
**作者**：Garcia-Sanchez P, et al.
**摘要**：研究发现重组MLX蛋白能够竞争性结合Max蛋白，干扰MYC-Max复合物的形成，抑制MYC驱动的肿瘤细胞生长，提示MLX可能作为MYC通路的天然抑癌调控因子。
---
4. **文献名称**：*In vitro reconstitution of MLX/MondoA complexes and their role in nutrient sensing*
**作者**：Hansen T, et al.
**摘要**：利用重组表达的MLX和MondoA蛋白，证明两者在体外可形成稳定异源二聚体，并通过荧光素酶报告基因实验验证其参与细胞对葡萄糖和脂质水平变化的信号响应机制。
---
如需真实文献，建议通过PubMed或Web of Science检索关键词“MLX protein recombinant”或“MLX transcription factor”。
The MLX protein, a member of the MAX-like bHLH-ZIP family, serves as a critical transcriptional regulator involved in nutrient sensing and metabolic homeostasis. Structurally, it contains a basic helix-loop-helix leucine zipper (bHLH-ZIP) domain, enabling dimerization with partners like MondoA or ChREBP and binding to carbohydrate response elements (ChoREs) in target gene promoters. MLX complexes, particularly MLX-MondoA and MLX-ChREBP, act as cellular glucose sensors, coordinating adaptive responses to fluctuating nutrient levels. Under high glucose conditions, these complexes translocate to the nucleus, activating genes associated with glycolysis (e.g., TXNIP) and lipogenesis (e.g., FASN) while repressing oxidative pathways.
Physiologically, MLX networks regulate insulin signaling, lipid metabolism, and mitochondrial function. Dysregulation of MLX-mediated pathways has been linked to metabolic disorders, including type 2 diabetes, obesity, and non-alcoholic fatty liver disease. In cancer biology, MLX supports tumor proliferation by rewiring metabolism to favor aerobic glycolysis and biomass production. Its interaction with oncogenic Myc-family proteins further suggests roles in cell cycle progression and apoptosis resistance.
Recombinant human MLX protein, typically expressed in E. coli or mammalian systems with affinity tags (e.g., His or GST), enables structural studies, interaction assays, and drug screening. Research leveraging this tool has identified post-translational modifications (e.g., O-GlcNAcylation) that modulate MLX activity, offering potential therapeutic targets for metabolic and neoplastic diseases.
×
