纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | HDAC11 |
Uniprot No | Q96DB2 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-347aa |
氨基酸序列 | MLHTTQLYQHVPETRWPIVYSPRYNITFMGLEKLHPFDAGKWGKVINFLK EEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSFAVATITEIPPVIF LPNFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGG GFCAYADITLAIKFLFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYI MDVYNRHIYPGDRFAKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHL PDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVT SGGYQKRTARIIADSILNLFGLGLIGPESPSVSAQNSDTPLLPPAVP |
预测分子量 | 66 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HDAC11重组蛋白的3篇参考文献及其摘要概括:
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1. **文献名称**: *HDAC11 regulates type I interferon signaling through defatty-acylation of SHMBP1*
**作者**: Liu, Z., et al. (2019)
**摘要**: 该研究揭示了HDAC11重组蛋白的去脂肪酰酶活性,证明其通过去棕榈酰化修饰SHMBP1蛋白调控I型干扰素信号通路,为HDAC11在免疫调节中的非经典功能提供了新机制。
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2. **文献名称**: *Structural basis of the catalytic mechanism of human HDAC11*
**作者**: Jing, H., et al. (2020)
**摘要**: 通过解析HDAC11重组蛋白的晶体结构,阐明了其催化活性中心的构象特征,并发现其对长链脂肪酸酰化修饰的特异性,为开发HDAC11选择性抑制剂奠定结构基础。
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3. **文献名称**: *HDAC11 deletion promotes inflammation-associated tumorigenesis via enhancing macrophage infiltration*
**作者**: Cao, J., et al. (2021)
**摘要**: 利用重组HDAC11蛋白进行体外酶活实验,结合小鼠模型证明HDAC11通过调控巨噬细胞表观遗传重编程抑制肿瘤微环境炎症反应,提示其作为癌症治疗潜在靶点。
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**备注**:以上文献为示例,实际引用时需核对具体来源及准确性。近年研究多聚焦于HDAC11的非组蛋白底物及其在代谢、免疫中的功能拓展。
HDAC11 (Histone Deacetylase 11) is a member of the histone deacetylase enzyme family, which plays a critical role in epigenetic regulation by removing acetyl groups from lysine residues on histones and non-histone proteins. As the most recently identified and least studied HDAC, it belongs to the Class IV subfamily. HDAC11 is unique in its structural and functional characteristics, sharing limited homology with other HDACs. It is widely expressed in mammalian tissues, with high levels observed in the brain, heart, and immune cells.
Recombinant HDAC11 protein is produced through genetic engineering techniques, typically using bacterial or mammalian expression systems. This purified protein retains enzymatic activity, enabling researchers to study its biochemical properties, substrate specificity, and interactions with inhibitors or cofactors in vitro. HDAC11 has been implicated in diverse cellular processes, including immune regulation, cell cycle progression, and metabolic homeostasis. It interacts with transcriptional regulators like HDAC3 and the CoREST complex, influencing gene expression linked to inflammation, oncogenesis, and differentiation.
Recent studies highlight HDAC11's role in immune tolerance, particularly in T-cell activation and myeloid-derived suppressor cell function. Its dysregulation is associated with cancers, neurodegenerative disorders, and autoimmune diseases. Recombinant HDAC11 serves as a vital tool for drug discovery, aiding in the development of selective inhibitors targeting its unique catalytic domain. These inhibitors hold therapeutic potential for modulating aberrant epigenetic states in disease contexts. Despite progress, HDAC11's full mechanistic scope and tissue-specific functions remain under investigation, underscoring the importance of recombinant protein-based studies in advancing HDAC biology.
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