| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | JMJD1C |
| Uniprot No | Q15652 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2274-2498aa |
| 氨基酸序列 | MPARYEDLLKSLPLPEYCNPEGKFNLASHLPGFFVRPDLGPRLCSAYGVVAAKDHDIGTTNLHIEVSDVVNILVYVGIAKGNGILSKAGILKKFEEEDLDDILRKRLKDSSEIPGALWHIYAGKDVDKIREFLQKISKEQGLEVLPEHDPIRDQSWYVNKKLRQRLLEEYGVRTCTLIQFLGDAIVLPAGALHQVQNFHSCIQVTEDFVSPEHLVESFHLTQELR |
| 预测分子量 | 45.5 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JMJD1C重组蛋白的3篇代表性文献(注：内容基于领域内相关研究综合概括，非真实文献，实际引用请查询具体数据库)：
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1. **文献名称**：*JMJD1C demethylates H3K9me2 to regulate estrogen receptor α target genes in breast cancer*
**作者**：Smith A, et al.
**摘要**：本研究利用重组JMJD1C蛋白进行体外酶活分析，证实其特异性去除组蛋白H3K9me2修饰。通过ChIP-seq发现JMJD1C通过去甲基化促进雌激素受体α(ERα)靶基因的转录激活，在乳腺癌细胞增殖中起关键作用。
2. **文献名称**：*Structural insights into JMJD1C-mediated histone demethylation and its interaction with LSD1*
**作者**：Zhang Y, et al.
**摘要**：通过重组JMJD1C蛋白的晶体结构解析，揭示了其JmjC结构域催化H3K9me2去甲基化的分子机制。进一步发现JMJD1C与LSD1形成复合物，协同调控基因沉默和白血病细胞分化。
3. **文献名称**：*JMJD1C regulates lipid metabolism by modulating PPARγ activity through enzymatic and non-enzymatic mechanisms*
**作者**：Tanaka K, et al.
**摘要**：利用重组JMJD1C蛋白进行功能实验，证明其通过去甲基化H3K9me2和直接结合PPARγ双重途径激活脂肪生成相关基因，影响肥胖及代谢综合征进程。
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**提示**：如需真实文献，建议在PubMed或Web of Science中检索关键词“JMJD1C recombinant protein”或“JMJD1C histone demethylase”，筛选涉及重组蛋白表达、功能或结构的研究。
JMJD1C, a member of the Jumonji C (JmjC) domain-containing protein family, is a histone demethylase implicated in epigenetic regulation. It catalyzes the removal of methyl groups from specific lysine residues on histones, primarily targeting dimethylated or monomethylated histone H3 lysine 9 (H3K9me2/1), though its substrate specificity may vary depending on cellular context. This enzymatic activity links JMJD1C to chromatin remodeling, transcriptional activation, and the dynamic control of gene expression. The protein contains several functional domains, including the catalytic JmjC domain, JmjN domain, and zinc-finger motifs, which facilitate interactions with chromatin and other regulatory proteins.
JMJD1C plays diverse roles in cellular processes such as stem cell maintenance, differentiation, and metabolic regulation. Studies highlight its involvement in tumorigenesis, where it can act as an oncogene or tumor suppressor depending on the cancer type. For example, JMJD1C promotes survival in acute myeloid leukemia by regulating genes critical for leukemic cell proliferation, while its loss is associated with genomic instability in certain solid tumors. Beyond cancer, JMJD1C is essential for adipogenesis, energy homeostasis, and neuronal development, underscoring its broad physiological relevance.
Recombinant JMJD1C protein is generated using expression systems like bacteria, insect cells, or mammalian cells to ensure proper post-translational modifications. This tool enables in vitro studies of its enzymatic kinetics, substrate preferences, and interactions with cofactors like α-ketoglutarate and iron. Researchers also use it to screen inhibitors for therapeutic development. Despite progress, questions remain about its context-dependent roles, tissue-specific regulation, and interplay with other epigenetic modifiers, making JMJD1C a focus of ongoing investigation in epigenetics and disease biology.
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