| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNMT3A |
| Uniprot No | Q9Y6K1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-912aa |
| 氨基酸序列 | MPAMPSSGPGDTSSSAAEREEDRKDGEEQEEPRGKEERQEPSTTARKVGR PGRKRKHPPVESGDTPKDPAVISKSPSMAQDSGASELLPNGDLEKRSEPQ PEEGSPAGGQKGGAPAEGEGAAETLPEASRAVENGCCTPKEGRGAPAEAG KEQKETNIESMKMEGSRGRLRGGLGWESSLRQRPMPRLTFQAGDPYYISK RKRDEWLARWKREAEKKAKVIAGMNAVEENQGPGESQKVEEASPPAVQQP TDPASPTVATTPEPVGSDAGDKNATKAGDDEPEYEDGRGFGIGELVWGKL RGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSF CSAFHQATYNKQPMYRKAIYEVLQVASSRAGKLFPVCHDSDESDTAKAVE VQNKPMIEWALGGFQPSGPKGLEPPEEEKNPYKEVYTDMWVEPEAAAYAP PPPAKKPRKSTAEKPKVKEIIDERTRERLVYEVRQKCRNIEDICISCGSL NVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCG NNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRRED WPSRLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVL KDLGIQVDRYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGP FDLVIGGSPCNDLSIVNPARKGLYEGTGRLFFEFYRLLHDARPKEGDDRP FFWLFENVVAMGVSDKRDISRFLESNPVMIDAKEVSAAHRARYFWGNLPG MNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSIKQGKDQHFPV FMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRH LFAPLKEYFACV |
| 预测分子量 | 162 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. |
1. **"Structure of DNMT3A bound to DNMT3L suggests a model for de novo DNA methylation"**
- **Authors**: Jia, D., Jurkowska, R.Z., Zhang, X. et al.
- **摘要**: 该研究通过X射线晶体学解析了DNMT3A与辅助因子DNMT3L的复合物结构，揭示了其催化结构域如何识别未甲基化的DNA并通过协同作用实现**从头甲基化**的分子机制，为表观遗传调控提供了结构基础。
2. **"Biochemical analysis of the recombinant human DNA methyltransferase DNMT3A"**
- **Authors**: Gowher, H., Jeltsch, A.
- **摘要**: 文章报道了重组人源DNMT3A蛋白的体外表达、纯化及酶活性分析，发现其甲基转移酶活性依赖于底物DNA的构象及与DNMT3L的相互作用，并揭示了其底物特异性的调控机制。
3. **"DNMT3A mutations in acute myeloid leukemia"**
- **Authors**: Yang, L., Rau, R., Goodell, M.A.
- **摘要**: 研究通过功能实验分析了白血病相关DNMT3A突变体(如R882H)对重组蛋白活性的影响，发现突变导致异常的DNA甲基化模式，进而驱动造血干细胞的恶性转化。
4. **"The DNMT3A ADD domain recognizes histone H3K4 unmethylated and regulates DNA methylation"**
- **Authors**: Zhang, Y., Jurkowska, R., Soeroes, S. et al.
- **摘要**: 该研究证明重组DNMT3A的ADD结构域特异性识别未甲基化的组蛋白H3K4.并阐明了这一互作如何调控DNMT3A在染色质上的靶向定位及甲基化活性。
以上文献涵盖DNMT3A重组蛋白的结构、酶学特性、病理突变效应及表观遗传调控机制等方向。
DNMT3A (DNA methyltransferase 3A) is a critical enzyme involved in establishing de novo DNA methylation patterns during mammalian development. As a member of the DNA methyltransferase family, it catalyzes the transfer of methyl groups to cytosine residues in CpG dinucleotides, a process essential for epigenetic regulation, genomic imprinting, and X-chromosome inactivation. Unlike DNMT1. which maintains methylation during DNA replication, DNMT3A acts predominantly during early embryogenesis and germ cell maturation to set up tissue-specific methylation profiles.
The DNMT3A protein contains a conserved C-terminal catalytic domain responsible for methyltransferase activity and an N-terminal regulatory region with PWWP and ADD domains that mediate chromatin targeting, protein interactions, and allosteric regulation. Its function is often modulated by interaction with DNMT3L, a catalytically inactive cofactor that enhances enzymatic activity. Recombinant DNMT3A proteins are commonly produced in expression systems like *E. coli* or insect cells for biochemical and structural studies. These purified proteins retain enzymatic activity and are used to investigate methylation kinetics, substrate specificity, and responses to inhibitors.
Mutations in DNMT3A are linked to developmental disorders and cancers, particularly acute myeloid leukemia (AML) and clonal hematopoiesis. The R882 hotspot mutation, for instance, disrupts normal methylation patterns and promotes oncogenesis. Recombinant mutant DNMT3A proteins have become vital tools for dissecting these disease mechanisms. Additionally, DNMT3A-targeted inhibitors are being explored for epigenetic therapies. Research on recombinant DNMT3A continues to advance our understanding of DNA methylation dynamics, offering insights into gene silencing, cellular differentiation, and potential therapeutic interventions for epigenetic diseases.
×
