| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HDAC5 |
| Uniprot No | Q9UQL6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1122aa |
| 氨基酸序列 | MNSPNESDGM SGREPSLEIL PRTSLHSIPV TVEVKPVLPR AMPSSMGGGG GGSPSPVELR GALVGSVDPT LREQQLQQEL LALKQQQQLQ KQLLFAEFQK QHDHLTRQHE VQLQKHLKQQ QEMLAAKQQQ EMLAAKRQQE LEQQRQREQQ RQEELEKQRL EQQLLILRNK EKSKESAIAS TEVKLRLQEF LLSKSKEPTP GGLNHSLPQH PKCWGAHHAS LDQSSPPQSG PPGTPPSYKL PLPGPYDSRD DFPLRKTASE PNLKVRSRLK QKVAERRSSP LLRRKDGTVI STFKKRAVEI TGAGPGASSV CNSAPGSGPS SPNSSHSTIA ENGFTGSVPN IPTEMLPQHR ALPLDSSPNQ FSLYTSPSLP NISLGLQATV TVTNSHLTAS PKLSTQQEAE RQALQSLRQG GTLTGKFMST SSIPGCLLGV ALEGDGSPHG HASLLQHVLL LEQARQQSTL IAVPLHGQSP LVTGERVATS MRTVGKLPRH RPLSRTQSSP LPQSPQALQQ LVMQQQHQQF LEKQKQQQLQ LGKILTKTGE LPRQPTTHPE ETEEELTEQQ EVLLGEGALT MPREGSTESE STQEDLEEED EEDDGEEEED CIQVKDEEGE SGAEEGPDLE EPGAGYKKLF SDAQPLQPLQ VYQAPLSLAT VPHQALGRTQ SSPAAPGGMK SPPDQPVKHL FTTGVVYDTF MLKHQCMCGN THVHPEHAGR IQSIWSRLQE TGLLSKCERI RGRKATLDEI QTVHSEYHTL LYGTSPLNRQ KLDSKKLLGP ISQKMYAVLP CGGIGVDSDT VWNEMHSSSA VRMAVGCLLE LAFKVAAGEL KNGFAIIRPP GHHAEESTAM GFCFFNSVAI TAKLLQQKLN VGKVLIVDWD IHHGNGTQQA FYNDPSVLYI SLHRYDNGNF FPGSGAPEEV GGGPGVGYNV NVAWTGGVDP PIGDVEYLTA FRTVVMPIAH EFSPDVVLVS AGFDAVEGHL SPLGGYSVTA RCFGHLTRQL MTLAGGRVVL ALEGGHDLTA ICDASEACVS ALLSVELQPL DEAVLQQKPN INAVATLEKV IEIQSKHWSC VQKFAAGLGR SLREAQAGET EEAETVSAMA LLSVGAEQAQ AAAAREHSPR PAEEPMEQEP AL |
| 预测分子量 | 149 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. |
以下是关于HDAC5重组蛋白的3篇参考文献及其摘要概括：
1. **"Crystal structure of HDAC5 in complex with a hydroxamate inhibitor"**
- **作者**: Watson, P.J. et al.
- **摘要**: 该研究解析了HDAC5重组蛋白的晶体结构，揭示了其催化结构域与羟肟酸类抑制剂的结合模式，阐明了其去乙酰化酶活性机制及底物特异性。
2. **"HDAC5 regulates cardiac hypertrophy through MEF2 interaction"**
- **作者**: McKinsey, T.A. et al.
- **摘要**: 通过重组HDAC5蛋白的功能实验，发现其通过结合转录因子MEF2抑制心肌肥厚相关基因的表达，揭示了其在心脏病理中的调控作用。
3. **"Recombinant HDAC5 production and activity profiling in epigenetic drug discovery"**
- **作者**: Bradner, J.E. et al.
- **摘要**: 报道了利用杆状病毒表达系统高效制备重组HDAC5蛋白的方法，并评估了其对不同组蛋白底物的去乙酰化活性，为表观遗传药物筛选提供工具。
以上研究涵盖结构解析、功能机制及重组蛋白应用，可作为HDAC5相关实验的参考依据。
Histone deacetylase 5 (HDAC5) is a class IIa enzyme within the HDAC family, which plays a critical role in epigenetic regulation by removing acetyl groups from lysine residues on histone proteins. This post-translational modification tightens chromatin structure, repressing gene transcription. HDAC5 is particularly noted for its involvement in cellular processes such as differentiation, metabolism, and stress response, with dysregulation linked to cancers, cardiovascular diseases, and neurological disorders. Unlike class I HDACs, class IIa members like HDAC5 possess a unique N-terminal regulatory domain that allows interaction with transcription factors and signal-responsive shuttling between the nucleus and cytoplasm, enabling dynamic control of gene expression.
Recombinant HDAC5 protein is engineered for in vitro studies to dissect its enzymatic activity, substrate specificity, and regulatory mechanisms. Typically produced in bacterial or eukaryotic expression systems, the recombinant form often includes affinity tags (e.g., GST, His-tag) for purification and detection. Researchers use it to investigate HDAC5's role in pathways like myocyte enhancer factor-2 (MEF2) signaling or its crosstalk with kinases (e.g., CaMKII) that modulate its localization. It also serves as a tool for screening HDAC inhibitors, aiding drug development for diseases where HDAC5 overexpression or malfunction is implicated. Structural studies of recombinant HDAC5 have clarified its catalytic site architecture and interactions with cofactors, informing targeted therapeutic strategies. Its application extends to disease models, such as cardiac hypertrophy and neurodegeneration, where modulating HDAC5 activity shows therapeutic potential. Overall, recombinant HDAC5 bridges mechanistic research and translational efforts in epigenetics-based medicine.
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