纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | HDAC10 |
Uniprot No | Q969S8 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-482aa |
氨基酸序列 | MGTALVYHEDMTATRLLWDDPECEIERPERLTAALDRLRQRGLEQRCLRL SAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIYFHPSTF HCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNV AIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYEHG RFWPFLRESDADAVGRGQGLGFTVNLPWNQVGMGNADYVAAFLHLLLPLA FEFDPELVLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRVCAV LEGGYHLESLAESVCMTVQTLLGDPAPPLSGPMAPCQSALESIQSARAAQ APHWKSLQQQDVTAVPMSPSSHSPEGRPPPLLPGGPVCKAAASAPSSLLD QPCLCPAPSVRTAVALTTPDITLVLPPDVIQQEASALREETEAWARPHES LAREEALTALGKLLYLLDGMLDGQVNSGIAAT |
预测分子量 | 71 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HDAC10重组蛋白的参考文献示例,包括文献名称、作者及摘要概括:
1. **"HDAC10 is a polyamine deacetylase"**
**作者**: Bheda et al. (2017)
**摘要**: 通过重组HDAC10蛋白的生化实验,发现其特异性催化多胺的脱乙酰化作用,而非传统组蛋白底物,揭示了其在细胞代谢中的独特功能。
2. **"Structural and functional analysis of human HDAC10"**
**作者**: Li et al. (2020)
**摘要**: 利用重组HDAC10蛋白进行晶体结构解析和酶动力学研究,阐明其催化机制及与底物结合的关键结构域,为靶向药物设计提供依据。
3. **"HDAC10 Recombinant Protein Modulates Autophagy in Cancer Cells"**
**作者**: Smith et al. (2019)
**摘要**: 研究显示,重组HDAC10蛋白通过调控自噬相关基因的表达,影响肿瘤细胞的存活和化疗耐药性,提示其作为癌症治疗的潜在靶点。
4. **"Development of a High-Throughput Screening Platform for HDAC10 Inhibitors"**
**作者**: Johnson et al. (2021)
**摘要**: 基于重组HDAC10蛋白建立高通量筛选体系,鉴定出多个选择性小分子抑制剂,并验证其在神经母细胞瘤模型中的抗增殖活性。
(注:以上文献为示例性质,实际引用时建议通过学术数据库核实具体信息。)
HDAC10. a member of the histone deacetylase (HDAC) family, belongs to the subclass IIb of HDACs, which are critical regulators of epigenetic modifications and cellular homeostasis. Unlike many other HDACs, HDAC10 is characterized by a unique structural organization, featuring an N-terminal domain and a C-terminal catalytic domain with weak deacetylase activity. It primarily localizes to the cytoplasm but can shuttle to the nucleus, influencing diverse physiological processes such as gene expression, cell cycle progression, and stress response. HDAC10 is implicated in deacetylating both histone and non-histone substrates, though its substrate specificity remains less defined compared to other HDACs. Emerging studies highlight its role in autophagy, metabolic regulation, and immune modulation, often through interactions with partner proteins or by forming complexes with other HDACs.
Recombinant HDAC10 protein, typically produced in bacterial or mammalian expression systems, enables detailed biochemical and functional studies. Its production involves cloning the HDAC10 gene into expression vectors, followed by purification using affinity tags (e.g., His-tag) to ensure high purity and activity. This recombinant tool is pivotal for investigating enzymatic kinetics, substrate preferences, and inhibitor screening in drug discovery. Notably, HDAC10’s overexpression or dysfunction has been linked to cancers, neurodegenerative disorders, and immune diseases, making it a potential therapeutic target. Research using recombinant HDAC10 has also uncovered non-canonical roles, such as acting as a scaffold in protein complexes or modulating cellular stress pathways independent of its enzymatic activity. These insights advance understanding of HDAC10’s dual regulatory mechanisms and its broader impact on disease pathogenesis, guiding the development of isoform-specific HDAC inhibitors for precision medicine.
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