- 中文名称
HIST1H4A
- 英文名字
- HIST1H4A
- 供应商
- Nordic BioSite
- 产品货号
- NDC-BT-2EHCN8-100
- 产品报价
- ¥询价/100ul

- 产品说明书
- 点击查看
- 购买方式
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- 产品新闻

- 背景资料
- HIST1H4A(HIST1H4A),详情产看产品说明书
- 序列
- The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination . Histone acetylation occurs mainly on the amino-terminal tail domains of histones H2A (Lys5), H2B (Lys5, 12, 15, and 20), H3 (Lys9, 14, 18, 23, 27, 36 and 56), and H4 (Lys5, 8, 12, and 16) and is important for the regulation of histone deposition, transcriptional activation, DNA replication, recombination, and DNA repair . Hyper-acetylation of the histone tails neutralizes the positive charge of these domains and is believed to weaken histone-DNA and nucleosome-nucleosome interactions, thereby destabilizing chromatin structure and increasing the accessibility of DNA to various DNA-binding proteins . In addition, acetylation of specific lysine residues creates docking sites for a protein module called the bromodomain, which binds to acetylated lysine residues . Many transcription and chromatin regulatory proteins contain bromodomains and may be recruited to gene promoters, in part, through binding of acetylated histone tails. Histone acetylation is mediated by histone acetyltransferases (HATs), such as CBP/p300, GCN5L2, PCAF, and Tip60, which are recruited to genes by DNA-bound protein factors to facilitate transcriptional activation . Deacetylation, which is mediated by histone deacetylases (HDAC and sirtuin proteins), reverses the effects of acetylation and generally facilitates transcriptional repression .
- 来源宿主
- The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination . Histone acetylation occurs mainly on the amino-terminal tail domains of histones H2A (Lys5), H2B (Lys5, 12, 15, and 20), H3 (Lys9, 14, 18, 23, 27, 36 and 56), and H4 (Lys5, 8, 12, and 16) and is important for the regulation of histone deposition, transcriptional activation, DNA replication, recombination, and DNA repair . Hyper-acetylation of the histone tails neutralizes the positive charge of these domains and is believed to weaken histone-DNA and nucleosome-nucleosome interactions, thereby destabilizing chromatin structure and increasing the accessibility of DNA to various DNA-binding proteins . In addition, acetylation of specific lysine residues creates docking sites for a protein module called the bromodomain, which binds to acetylated lysine residues . Many transcription and chromatin regulatory proteins contain bromodomains and may be recruited to gene promoters, in part, through binding of acetylated histone tails. Histone acetylation is mediated by histone acetyltransferases (HATs), such as CBP/p300, GCN5L2, PCAF, and Tip60, which are recruited to genes by DNA-bound protein factors to facilitate transcriptional activation . Deacetylation, which is mediated by histone deacetylases (HDAC and sirtuin proteins), reverses the effects of acetylation and generally facilitates transcriptional repression .
- 溶解建议
- WB: 1:500~1:1000
- 保存建议
- Store at 4
- 其他
- Nordic BioSite(北欧生物) 总部位于瑞典,成立于1997年,旨在分销研究和诊断领域的高质量和创新产品。 Nordic BioSite 被公认为整个北欧生物医学研究和诊断产品领域的领导者。他们拥有超过570万种的产品组合,代理了遍布欧洲和美国的顶级生物试剂制造商,是欧洲知名的一站式生物试剂代理商。除了作为分销商之外,Nordic BioSite 还拥有不断增长的自产产品线——BioSite mAb、BioSite ELISA、BioSite Flow、Optibodies和 BioSite Protein, 目前艾美捷代理的是Nordic BioSite自产产品线(共26W+产品)。Nordic BioSite的产品类型主要是抗体,蛋白和试剂盒,产品适用范围涵盖15个不同的物种(人,牛,犬,鲶鱼,鸡,海豚,马,猫,豚鼠,小鼠,绵羊,兔子,大鼠,猪和火鸡),可为您提供一站式的生命科学研究解决方案~

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