| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HDAC7 |
| Uniprot No | Q8WUI4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 4-203aa |
| 氨基酸序列 | PGADGTQVSPGAHYCSPTGAGCPRPCADTPGPQPQPMDLRVGQRPPVEPPPEPTLLALQRPQRLHHHLFLAGLQQQRSVEPMRLSMDTPMPELQVGPQEQELRQLLHKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPNSPGIPYRTLEPLETEGATRSMLSSFLPPVPSLPSDPPEHFPLRKTVSEPNLKLRYK |
| 预测分子量 | 26 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. |
以下为基于HDAC7重组蛋白相关研究方向的示例性参考文献(内容为模拟概括，建议通过学术数据库核实准确信息)：
1. **"HDAC7 regulates apoptosis in developing thymocytes via modulation of β-catenin"**
*作者: Dequiedt F et al.*
摘要：研究揭示了HDAC7通过调控β-catenin的乙酰化状态影响胸腺细胞凋亡，利用重组HDAC7蛋白证明其直接与β-catenin相互作用，并调节T细胞发育过程中的生存信号通路。
2. **"Structural basis for the deacetylase activity of HDAC7"**
*作者: Wang Z et al.*
摘要：通过重组HDAC7蛋白的晶体结构解析，阐明了其催化结构域的关键氨基酸残基及底物识别机制，为设计选择性HDAC抑制剂提供结构生物学依据。
3. **"HDAC7-mediated repression of matrix metalloproteinases in vascular smooth muscle cells"**
*作者: Chang S et al.*
摘要：研究发现重组HDAC7蛋白通过去乙酰化作用抑制MMP基因表达，调节血管平滑肌细胞迁移及动脉粥样硬化进程，提示其作为心血管疾病治疗靶点。
4. **"In vitro reconstitution of HDAC7-3-phosphoinositide-dependent kinase 1 complex"**
*作者: Parra M et al.*
摘要：利用重组蛋白技术证明HDAC7与PDK1的物理结合依赖其磷酸化状态，并揭示了该复合物在胰岛素信号转导中的调控作用。
**注意**：以上文献信息为示例性概括，实际引用需通过PubMed/ScienceDirect等平台验证作者、标题及摘要准确性。建议结合关键词“HDAC7 recombinant protein”“structure/function”等进行精准检索。
HDAC7 (Histone Deacetylase 7) is a member of the class IIa HDAC family, a group of enzymes critical for epigenetic regulation by removing acetyl groups from histone proteins, thereby modulating chromatin structure and gene expression. As a key player in transcriptional repression, HDAC7 interacts with transcription factors and corepressor complexes (e.g., NCOR/SMRT) to silence target genes. It is uniquely characterized by its tissue-specific expression, predominantly in endothelial cells, T lymphocytes, and muscle cells, where it regulates differentiation, apoptosis, and vascular development. Structurally, HDAC7 contains an N-terminal regulatory domain with binding sites for partner proteins and a C-terminal catalytic domain, though its intrinsic deacetylase activity is weak compared to other HDACs, requiring association with other enzymes for full functionality.
Recombinant HDAC7 protein is engineered for in vitro studies to dissect its biochemical properties, enzymatic mechanisms, and interactions. Produced using expression systems like *E. coli* or mammalian cells, the recombinant form often includes affinity tags (e.g., GST, His-tag) for purification. Researchers employ it to investigate post-translational modifications (e.g., phosphorylation, ubiquitination) that regulate its nucleo-cytoplasmic shuttling and activity. Additionally, it serves as a tool for screening HDAC inhibitors or studying its role in diseases. Dysregulation of HDAC7 is linked to cancers, cardiovascular disorders, and immune dysfunction, making it a potential therapeutic target. Recombinant HDAC7 enables mechanistic studies, such as its involvement in angiogenesis via VEGF signaling or T-cell tolerance through FOXP3 interactions. Despite its limited standalone enzymatic activity, its scaffold function in multi-protein complexes underscores its biological significance, driving demand for high-purity recombinant protein to advance both basic research and drug discovery.
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