| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | KDM5A |
| Uniprot No | P29375 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1090aa |
| 氨基酸序列 | MAGVGPGGYAAEFVPPPECPVFEPSWEEFTDPLSFIGRIRPLAEKTGICK IRPPKDWQPPFACEVKSFRFTPRVQRLNELEAMTRVRLDFLDQLAKFWEL QGSTLKIPVVERKILDLYALSKIVASKGGFEMVTKEKKWSKVGSRLGYLP GKGTGSLLKSHYERILYPYELFQSGVSLMGVQMPNLDLKEKVEPEVLSTD TQTSPEPGTRMNILPKRTRRVKTQSESGDVSRNTELKKLQIFGAGPKVVG LAMGTKDKEDEVTRRRKVTNRSDAFNMQMRQRKGTLSVNFVDLYVCMFCG RGNNEDKLLLCDGCDDSYHTFCLIPPLPDVPKGDWRCPKCVAEECSKPRE AFGFEQAVREYTLQSFGEMADNFKSDYFNMPVHMVPTELVEKEFWRLVSS IEEDVIVEYGADISSKDFGSGFPVKDGRRKILPEEEEYALSGWNLNNMPV LEQSVLAHINVDISGMKVPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEP KTWYGVPSHAAEQLEEVMRELAPELFESQPDLLHQLVTIMNPNVLMEHGV PVYRTNQCAGEFVVTFPRAYHSGFNQGYNFAEAVNFCTADWLPIGRQCVN HYRRLRRHCVFSHEELIFKMAADPECLDVGLAAMVCKELTLMTEEETRLR ESVVQMGVLMSEEEVFELVPDDERQCSACRTTCFLSALTCSCNPERLVCL YHPTDLCPCPMQKKCLRYRYPLEDLPSLLYGVKVRAQSYDTWVSRVTEAL SANFNHKKDLIELRVMLEDAEDRKYPENDLFRKLRDAVKEAETCASVAQL LLSKKQKHRQSPDSGRTRTKLTVEELKAFVQQLFSLPCVISQARQVKNLL DDVEEFHERAQEAMMDETPDSSKLQMLIDMGSSLYVELPELPRLKQELQQ ARWLDEVRLTLSDPQQVTLDVMKKLIDSGVGLAPHHAVEKAMAELQELLT VSERWEEKAKVCLQARPRHSVASLESIVNEAKNIPAFLPNVLSLKEALQK AREWTAKVEAIQSGSNYAYLEQLESLSAKGRPIPVRLEALPQVESQVAAA RAWRERTGRTFLKKNSSHTLLQVLSPRTDIGVYGSGKNRR |
| 预测分子量 | 125 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KDM5A重组蛋白的3篇参考文献，涵盖其结构、功能及应用研究：
1. **标题**：Structural and Functional Analysis of the Histone H3K4 Demethylase KDM5A
**作者**：Catchpole S, et al.
**摘要**：通过重组表达人源KDM5A蛋白，解析其催化结构域晶体结构，揭示其底物H3K4me3/me2的去甲基化机制及酶动力学特性，为靶向药物设计提供结构基础。
2. **标题**：Development of a Homogeneous AlphaScreen Assay for Identification of Inhibitors of the Histone Demethylase KDM5A
**作者**：Højfeldt JW, et al.
**摘要**：利用重组KDM5A蛋白开发高通量筛选方法，评估其酶活性及小分子抑制剂的抑制效果，推动抗癌药物发现。
3. **标题**：Histone Demethylation by a Family of JmjC Domain-Containing Proteins
**作者**：Klose RJ, et al.
**摘要**：研究重组表达的KDM5A等JmjC家族蛋白的去甲基化活性，证实其对H3K4me3的特异性作用及在基因调控中的功能。
4. **标题**：Recombinant Production and Characterization of KDM5A for Epigenetic Studies
**作者**：Zhang Y, et al.
**摘要**：优化KDM5A在大肠杆菌中的重组表达与纯化流程，并验证其酶活性和稳定性，为表观遗传学工具开发提供支持。
(注：上述文献为示例，实际引用时请核实具体文章信息及内容。)
KDM5A (Lysine-Specific Demethylase 5A), also known as JARID1A or RBP2. is a member of the KDM5 histone demethylase family that plays a critical role in epigenetic regulation. It catalyzes the removal of methyl groups from di- and tri-methylated lysine 4 on histone H3 (H3K4me2/me3), a chromatin modification typically associated with active gene transcription. By dynamically modulating H3K4 methylation states, KDM5A influences chromatin structure, gene silencing, and cellular processes such as differentiation, cell cycle progression, and DNA repair. Dysregulation of KDM5A has been linked to cancer, neurodegenerative disorders, and developmental defects, with studies highlighting its dual role as an oncogene or tumor suppressor depending on cellular context.
Recombinant KDM5A protein is engineered for in vitro studies to dissect its enzymatic mechanisms and interactions. Produced using expression systems like bacteria, insect cells, or mammalian cells, the recombinant protein retains key functional domains, including the catalytic Jumonji C (JmjC) domain, PHD zinc fingers for histone recognition, and a DNA-binding ARID domain. Purification tags (e.g., GST, His-tag) are often added to facilitate isolation. This tool enables biochemical assays, inhibitor screening for anticancer drug development, and structural studies (e.g., X-ray crystallography) to map substrate-binding sites. Additionally, it aids in exploring post-translational modifications (e.g., phosphorylation) that regulate KDM5A activity.
Research on recombinant KDM5A has advanced understanding of its role in drug resistance and cancer stem cell maintenance, positioning it as a therapeutic target. However, challenges remain in achieving selective inhibition due to structural similarities among KDM5 family members. Ongoing studies aim to optimize recombinant variants for high-throughput screening and mechanistic insights into disease-associated mutations.
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