| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | KDM4A |
| Uniprot No | O75164 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-886aa |
| 氨基酸序列 | MASESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPKEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQYNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWKNLTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFATRRWIEYGKQAVLCSCRKDMVKISMDVFVRKFQPERYKLWKAGKDNTVIDHTLPTPEAAEFLKESELPPRAGNEEECPEEDMEGVEDGEEGDLKTSLAKHRIGTKRHRVCLEIPQEVSQSELFPKEDLSSEQYEMTECPAALAPVRPTHSSVRQVEDGLTFPDYSDSTEVKFEELKNVKLEEEDEEEEQAAAALDLSVNPASVGGRLVFSGSKKKSSSSLGSGSSRDSISSDSETSEPLSCRAQGQTGVLTVHSYAKGDGRVTVGEPCTRKKGSAARSFSERELAEVADEYMFSLEENKKSKGRRQPLSKLPRHHPLVLQECVSDDETSEQLTPEEEAEETEAWAKPLSQLWQNRPPNFEAEKEFNETMAQQAPHCAVCMIFQTYHQVEFGGFNQNCGNASDLAPQKQRTKPLIPEMCFTSTGCSTDINLSTPYLEEDGTSILVSCKKCSVRVHASCYGVPPAKASEDWMCSRCSANALEEDCCLCSLRGGALQRANDDRWVHVSCAVAILEARFVNIAERSPVDVSKIPLPRFKLKCIFCKKRRKRTAGCCVQCSHGRCPTAFHVSCAQAAGVMMQPDDWPFVVFITCFRHKI |
| 预测分子量 | 150 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KDM4A重组蛋白的3篇示例参考文献(内容为虚构示例，仅供参考)：
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1. **文献名称**: *"Recombinant Expression and Enzymatic Characterization of Human Histone Demethylase KDM4A"*
**作者**: Smith J, et al.
**摘要**: 本研究通过大肠杆菌系统成功表达并纯化重组KDM4A蛋白，验证其特异性去除H3K9me3/me2的活性，并发现其酶活性依赖于Fe²⁺和α-酮戊二酸辅因子。
2. **文献名称**: *"Structural Insights into KDM4A Catalytic Domain by X-ray Crystallography"*
**作者**: Jones R, et al.
**摘要**: 解析了重组KDM4A催化结构域的晶体结构(分辨率2.1Å)，揭示其底物结合口袋的构象变化，为设计靶向抑制剂提供了结构基础。
3. **文献名称**: *"KDM4A Promotes Tumor Metastasis via Epigenetic Silencing of CDH1 in Breast Cancer"*
**作者**: Kim S, et al.
**摘要**: 利用重组KDM4A蛋白进行体外功能实验，证明其通过去甲基化抑制E-cadherin(CDH1)启动子区域H3K9甲基化，促进乳腺癌细胞侵袭。
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**提示**：实际文献建议通过PubMed、Google Scholar等平台，以关键词“KDM4A recombinant protein”“KDM4A purification”“KDM4A enzymatic activity”检索。真实研究多关注其结构、酶学特性及在癌症中的调控机制。
KDM4A (Lysine-Specific Demethylase 4A), also known as JMJD2A or JHDM3A, is a member of the Jumonji C (JmjC) domain-containing histone demethylase family. It catalyzes the removal of methyl groups from specific lysine residues on histones, primarily targeting trimethylated histone H3 lysine 9 (H3K9me3/me2) and H3 lysine 36 (H3K36me3/me2), using an Fe²⁺- and α-ketoglutarate-dependent oxidative reaction. This enzymatic activity enables KDM4A to regulate chromatin structure, gene transcription, and epigenetic inheritance. It plays critical roles in diverse cellular processes, including DNA replication, repair, cell cycle progression, and stem cell differentiation.
Recombinant KDM4A proteins are engineered versions of the enzyme produced in heterologous expression systems (e.g., E. coli, insect, or mammalian cells) for research and therapeutic applications. These proteins typically retain the conserved JmjN, JmjC, and Tudor domains essential for substrate recognition and catalytic activity. Researchers utilize recombinant KDM4A to study its demethylase mechanisms, interactions with chromatin-modifying complexes, and roles in diseases. Overexpression of KDM4A is implicated in cancers (e.g., prostate, breast), where it may promote oncogenesis by silencing tumor suppressors or inducing genomic instability through aberrant demethylation.
The development of recombinant KDM4A has accelerated drug discovery efforts, enabling high-throughput screening of inhibitors targeting its demethylase activity. Such inhibitors hold promise as epigenetic therapies to counteract KDM4A-driven malignancy. Additionally, recombinant proteins serve as tools to map histone modification landscapes and investigate crosstalk between epigenetic regulators. Despite progress, challenges remain in understanding tissue-specific functions and optimizing recombinant variants for structural studies. Ongoing research aims to elucidate KDM4A's full pathophysiological spectrum and leverage recombinant forms for precision epigenetics.
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