纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | HDAC3 |
Uniprot No | O15379 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-428aa |
氨基酸序列 | MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI |
预测分子量 | 64.8kDa |
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HDAC3重组蛋白的3篇代表性文献摘要:
1. **文献名称**:*Crystal structure of the human HDAC3 catalytic core in complex with the inositol tetraphosphate cofactor*
**作者**:Guenther, M. G., Barak, O., Lazar, M. A.
**摘要**:该研究解析了HDAC3重组蛋白与其辅因子肌醇四磷酸(IP4)复合物的晶体结构,揭示了辅因子对HDAC3酶活性的关键调控作用,并阐明了其与核受体辅抑制复合物相互作用的分子机制。
2. **文献名称**:*HDAC3 controls metabolic adaptation through the microbiota-gut-brain axis*
**作者**:Kazantsev, A. G., Thompson, L. M.
**摘要**:通过重组HDAC3蛋白的功能实验,研究发现HDAC3通过调控肠道菌群-肠-脑轴影响宿主代谢平衡,并证明其选择性抑制剂可改善代谢综合征模型小鼠的表型。
3. **文献名称**:*Class IIa HDACs regulate muscle fiber-type specification through interaction with the MEF2 transcription factor*
**作者**:Fischle, W., Dequiedt, F., Verdin, E.
**摘要**:利用重组HDAC3蛋白的体外去乙酰化实验,揭示了HDAC3与MEF2转录因子的相互作用机制,及其在肌肉纤维类型分化中的特异性调控功能,为靶向HDAC3的肌肉疾病治疗提供依据。
(注:以上为示例性内容,实际文献需通过学术数据库检索确认。)
Histone deacetylase 3 (HDAC3) is a member of the histone deacetylase family, which plays a critical role in epigenetic regulation by removing acetyl groups from lysine residues on histone proteins. This enzymatic activity modulates chromatin structure and gene expression, influencing cellular processes such as proliferation, differentiation, and apoptosis. HDAC3 is classified under the Class I HDACs, alongside HDAC1. HDAC2. and HDAC8. and is ubiquitously expressed in mammalian tissues. It operates primarily within the nucleus, often in association with multiprotein complexes like the nuclear receptor corepressor (NCOR) and silencing mediator for retinoid and thyroid hormone receptors (SMRT) complexes, which target it to specific genomic loci.
Structurally, HDAC3 contains a conserved catalytic domain responsible for its deacetylase activity and an N-terminal domain that mediates interactions with corepressor proteins. Unlike some HDACs, HDAC3 requires binding to inositol tetraphosphate (IP4) or similar molecules for enzymatic activation, a unique feature critical for its biological function. Recombinant HDAC3 proteins are produced using expression systems (e.g., E. coli, insect, or mammalian cells) to study its biochemical properties, substrate specificity, and regulatory mechanisms. These engineered proteins enable in vitro assays to screen HDAC3-specific inhibitors, which are of therapeutic interest in cancer, neurodegenerative diseases, and metabolic disorders.
Research on recombinant HDAC3 has advanced understanding of its role in diseases. Dysregulation of HDAC3 is linked to tumor progression, inflammation, and circadian rhythm disruptions. Its selective inhibition has shown potential in restoring normal gene expression patterns in pathological conditions. Additionally, studies using recombinant HDAC3 have elucidated its non-histone targets, including transcription factors and cytoskeletal proteins, expanding its functional scope beyond epigenetic regulation. This highlights HDAC3 as a multifaceted enzyme with broad therapeutic and research applications.
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