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Recombinant Mononucleosomes H3.2
Recombinant Mononucleosomes H3.2
- 中文名称：
- Recombinant Mononucleosomes H3.2
- 英文名称：
- Recombinant Mononucleosomes H3.2
- 品牌：
- AAA Biotech
- 品牌介绍：
- AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具，核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
- 货号：
- AAA60226
- 规格：
- 0.02 mg|1 mg|2x1 mg|3x1 mg|4x1 mg
- 保存建议：
- Recombinant proteins in solution are temperature sensitive and must be stored at -80 degree C to prevent degradation. Avoid repeated freeze/thaw cycles and keep on ice when not in storage.
Shipping Temp: Dry Ice
- 货期：
- 6-8周
- 纯度：
- N/A
- 产品形式：
- Recombinant Mononucleosomes H3.2 is supplied in 10mM Tris-HCl pH8.0, 1mM EDTA, 2mM DTT, and 20% glycerol.
- 免责声明：
- *本产品仅供科研实验使用，不得用于临床诊断。*
- 说明书：
Background: In vivo, histones are wrapped around by DNA in chromatin. Therefore, nucleosomes are more physiologically relevant substrates than histones and histone-derived peptides for in vitro studies. More importantly, some histone methyltransferases are signifcantly more active, as well as specifc, when using nucleosomal substrates in HMT assays, such as DOT1L and NSD family enzymes. Nucleosomes are also widely used in histone methyltransferase screening assays to identify small molecular inhibitors for drug discovery. Nuclear core histone H3 exist as several variants: H3.1, H3.2, H3.3, CENP-A and H3t. These variants have been suggested to have specific functions in the regulation of gene expression and genome stability. In mammals, histone H3 non-centromeric variants, H3.1, H3.2 and H3.3, differ in their chromatin deposition patterns and PTMs despite having a high degree of sequence similarity. H3.1 and H3.2, which are enriched in repressive chromatin marks, are predominantly expressed during S-Phase and deposited in DNA synthesis-coupled fashion during DNA replication and repair. In contrast, H3.3 is enriched in active chromatin marks and is expressed throughout the cell cycle. Canonical histone H3.2 is expressed during S phase and differs by only one amino acid residue from th variant histone H3.1, and four amino acid residues from histone H3.3. According to some researchers, H3.1 is preferentially acetylated and dimethylated on lysines 14 and 9, respectively, while H3.2 is preferentially subjected to trimethylation on lysine 27.
