- 中文名称
HIST1H2BC
- 英文名字
- HIST1H2BC
- 供应商
- Nordic BioSite
- 产品货号
- NDC-BT-0ANTSF-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
- HIST1H2BC(HIST1H2BC)，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. The p300/CBP histone acetyltransferases acetylate multiple lysine residues in the amino terminal tail of histone H2B (Lys5, 12, 15, and 20) at gene promoters during transcriptional activation. 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 access of DNA to various DNA-binding proteins. In addition, acetylation of specific lysine residues creates docking sites that facilitate recruitment of many transcription and chromatin regulatory proteins that contain a bromodomain, which binds to acetylated lysine residues. Histone H2B is mono-ubiquitinated at Lys120 during transcriptional activation by the RAD6 E2 protein in conjunction with the BRE1A/BRE1B E3 ligase (also known as RNF20/RNF40). Mono-ubiquitinated histone H2B Lys120 is associated with the transcribed region of active genes and stimulates transcriptional elongation by facilitating FACT-dependent chromatin remodeling. In addition, it is essential for subsequent methylation of histone H3 Lys4 and Lys79, two additional histone modifications that regulate transcriptional initiation and elongation. In response to metabolic stress, AMPK is recruited to responsive genes and phosphorylates histone H2B at Lys36, both at promoters and in transcribed regions of genes, and may regulate transcriptional elongation . In response to multiple apoptotic stimuli, histone H2B is phosphorylated at Ser14 by the Mst1 kinase . Upon induction of apoptosis, Mst1 is cleaved and activated by caspase-3, leading to global phosphorylation of histone H2B during chromatin condensation. Interestingly, histone H2B is rapidly phosphorylated at irradiation-induced DNA damage foci in mouse embryonic fibroblasts. In this case, phosphorylation at Ser14 is rapid, depends on prior phosphorylation of H2AX Ser139, and occurs in the absence of apoptosis, suggesting that Ser14 phosphorylation may have distinct roles in DNA-damage repair and apoptosis.
- 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. The p300/CBP histone acetyltransferases acetylate multiple lysine residues in the amino terminal tail of histone H2B (Lys5, 12, 15, and 20) at gene promoters during transcriptional activation. 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 access of DNA to various DNA-binding proteins. In addition, acetylation of specific lysine residues creates docking sites that facilitate recruitment of many transcription and chromatin regulatory proteins that contain a bromodomain, which binds to acetylated lysine residues. Histone H2B is mono-ubiquitinated at Lys120 during transcriptional activation by the RAD6 E2 protein in conjunction with the BRE1A/BRE1B E3 ligase (also known as RNF20/RNF40). Mono-ubiquitinated histone H2B Lys120 is associated with the transcribed region of active genes and stimulates transcriptional elongation by facilitating FACT-dependent chromatin remodeling. In addition, it is essential for subsequent methylation of histone H3 Lys4 and Lys79, two additional histone modifications that regulate transcriptional initiation and elongation. In response to metabolic stress, AMPK is recruited to responsive genes and phosphorylates histone H2B at Lys36, both at promoters and in transcribed regions of genes, and may regulate transcriptional elongation . In response to multiple apoptotic stimuli, histone H2B is phosphorylated at Ser14 by the Mst1 kinase . Upon induction of apoptosis, Mst1 is cleaved and activated by caspase-3, leading to global phosphorylation of histone H2B during chromatin condensation. Interestingly, histone H2B is rapidly phosphorylated at irradiation-induced DNA damage foci in mouse embryonic fibroblasts. In this case, phosphorylation at Ser14 is rapid, depends on prior phosphorylation of H2AX Ser139, and occurs in the absence of apoptosis, suggesting that Ser14 phosphorylation may have distinct roles in DNA-damage repair and apoptosis.
- 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~
- 注意
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