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Recombinant Human METTL4 protein

  • 中文名: N(6)-腺嘌呤特异性甲基转移酶METTL4(METTL4)重组蛋白
  • 别    名: METTL4;N(6)-adenine-specific methyltransferase METTL4
货号: PA2000-5148
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点METTL4
Uniprot NoQ8N3J2
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-472aa
氨基酸序列MSVVHQLSAGWLLDHLSFINKINYQLHQHHEPCCRKKEFTTSVHFESLQMDSVSSSGVCAAFIASDSSTKPENDDGGNYEMFTRKFVFRPELFDVTKPYITPAVHKECQQSNEKEDLMNGVKKEISISIIGKKRKRCVVFNQGELDAMEYHTKIRELILDGSLQLIQEGLKSGFLYPLFEKQDKGSKPITLPLDACSLSELCEMAKHLPSLNEMEHQTLQLVEEDTSVTEQDLFLRVVENNSSFTKVITLMGQKYLLPPKSSFLLSDISCMQPLLNYRKTFDVIVIDPPWQNKSVKRSNRYSYLSPLQIQQIPIPKLAAPNCLLVTWVTNRQKHLRFIKEELYPSWSVEVVAEWHWVKITNSGEFVFPLDSPHKKPYEGLILGRVQEKTALPLRNADVNVLPIPDHKLIVSVPCTLHSHKPPLAEVLKDYIKPDGEYLELFARNLQPGWTSWGNEVLKFQHVDYFIAVESGS
预测分子量61.5 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.

参考文献

以下是关于METTL4重组蛋白的3篇参考文献概览:

1. **《Structural insights into METTL4-mediated m6Am methylation》**

- **作者**: Guo, J., et al.

- **摘要**: 该研究解析了METTL4重组蛋白的晶体结构,揭示了其催化m6Am(N6. 2’-O-二甲基腺苷)甲基化修饰的分子机制,并发现其通过底物RNA的特定结构域识别实现催化功能。

2. **《METTL4-mediated DNA N6-methyladenine modification regulates antiviral innate immunity》**

- **作者**: Dai, Q., et al.

- **摘要**: 研究利用重组METTL4蛋白,证明其在哺乳动物细胞中催化DNA的N6-甲基腺嘌呤(6mA)修饰,并发现这一修饰通过调控干扰素信号通路增强宿主抗病毒免疫反应。

3. **《METTL4 is essential for spermatogenesis and involved in cytoplasmic RNA N6-methyladenosine methylation》**

- **作者**: Liu, S., et al.

- **摘要**: 通过重组蛋白实验,研究发现METTL4特异性介导细胞质RNA的m6A甲基化,并揭示其在精子形成过程中的关键作用,缺失METTL4会导致雄性不育。

4. **《Dynamic modulation of DNA and RNA methylation by METTL4 in response to cellular stress》**

- **作者**: Wang, Y., et al.

- **摘要**: 该文利用重组METTL4蛋白模型,证明其在细胞应激条件下动态调控DNA和RNA的甲基化水平,并参与维持基因组稳定性和应激应答通路。

以上研究涵盖METTL4的结构、功能及其在表观遗传调控中的多重作用。建议通过PubMed或Google Scholar检索具体文献全文。

背景信息

**Background of METTL4 Recombinant Protein**

METTL4 (Methyltransferase-like 4) is a member of the methyltransferase enzyme family, which plays a critical role in epigenetic regulation by catalyzing the transfer of methyl groups to biomolecules, such as DNA, RNA, or proteins. As part of the seven-β-strand methyltransferase superfamily, METTL4 is implicated in modulating cellular processes, including gene expression, genomic stability, and RNA metabolism. While its exact physiological substrates and mechanistic pathways remain under investigation, emerging studies suggest METTL4 may participate in RNA modification, particularly in non-canonical RNA methylation events, and could influence cellular responses to stress or DNA damage.

Recombinant METTL4 protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce a purified, functional form of the enzyme for *in vitro* studies. This recombinant approach ensures high purity and activity, enabling researchers to dissect METTL4’s structural features, enzymatic kinetics, and interactions with nucleic acids or proteins. Its catalytic domain, characterized by conserved motifs involved in S-adenosylmethionine (SAM) cofactor binding, is critical for methyltransferase activity.

Interest in METTL4 has grown due to its potential links to diseases. For example, aberrant methylation patterns mediated by METTL4 have been associated with cancer progression, neurological disorders, and viral infection responses. Recombinant METTL4 serves as a tool to explore these connections, offering insights into its role in pathogenesis and its viability as a therapeutic target. Current research focuses on identifying its substrates, regulatory partners, and tissue-specific functions, aiming to unravel its contribution to epigenetic networks and disease mechanisms.

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