| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MDFI |
| Uniprot No | Q99750 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-246aa |
| 活性数据 | MYQVSGQRPS GCDAPYGAPS AAPGPAQTLS LLPGLEVVTG STHPAEAAPE EGSLEEAATP MPQGNGPGIP QGLDSTDLDV PTEAVTCQPQ GNPLGCTPLL PNDSGHPSEL GGTRRAGNGA LGGPKAHRKL QTHPSLASQG SKKSKSSSKS TTSQIPLQAQ EDCCVHCILS CLFCEFLTLC NIVLDCATCG SCSSEDSCLC CCCCGSGECA DCDLPCDLDC GILDACCESA DCLEICMECC GLCFSS |
| 分子量 | 25 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MDFI蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：**"Functional analysis of recombinant human MDFI in MyoD-mediated transcriptional repression"**
**作者**：Gomes, B.C., et al.
**摘要**：本研究利用重组人MDFI蛋白，揭示了其通过结合MyoD转录因子并抑制其活性，从而调控骨骼肌细胞分化的分子机制。实验证实MDFI的C端结构域是抑制功能的关键区域。
2. **文献名称**：**"Recombinant expression and purification of human MDFI in Escherichia coli: A tool for studying its role in Hedgehog signaling"**
**作者**：Smith, J.L., et al.
**摘要**：报道了一种高效的大肠杆菌表达系统用于重组人MDFI蛋白的制备。纯化的蛋白可用于体外结合实验，证明MDFI通过抑制Gli转录因子(Hedgehog通路核心组分)影响胚胎发育过程。
3. **文献名称**：**"MDFI interacts with β-catenin via recombinant protein assays: Implications for Wnt signaling modulation"**
**作者**：Chen, H., et al.
**摘要**：通过重组人MDFI蛋白的体外实验，发现其直接结合β-catenin并拮抗Wnt信号通路，提示MDFI可能参与癌症发生中细胞增殖与分化的平衡调控。
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**注**：以上文献及内容为模拟情景下的概括，实际文献需通过学术数据库(如PubMed、Web of Science)检索确认。若需进一步探索，建议结合关键词“MDFI”、“recombinant protein”、“MyoD inhibitor”、“Hedgehog/Wnt signaling”进行查阅。
MDFI (MyoD family inhibitor), also known as I-mfa, is a human protein involved in regulating transcription and cellular differentiation. Structurally, it contains an N-terminal cysteine-rich domain (CRD) and a C-terminal half that interacts with basic helix-loop-helix (bHLH) transcription factors. Its primary function lies in suppressing myogenic differentiation by binding to and inhibiting MyoD family proteins through its CRD domain, effectively blocking their interaction with transcriptional coactivators like E-proteins. Beyond muscle development, MDFI modulates multiple signaling pathways (including Wnt/β-catenin and Hedgehog) by interacting with cytoplasmic components.
Recombinant human MDFI protein is typically produced in *E. coli* or mammalian expression systems, enabling studies on its structural-functional relationships and molecular mechanisms. Its therapeutic potential is being explored in cancer research due to its role in cell cycle regulation and tumor suppression. Additionally, it serves as a tool to investigate muscle regeneration, stem cell differentiation, and developmental biology. Recent studies also suggest its involvement in viral infection processes, highlighting broad interdisciplinary relevance. Researchers utilize purified MDFI protein for *in vitro* binding assays, crystallography, and pathway modulation experiments to decode its multifaceted biological roles.
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