Yoshimi Tomohiko, Ohkawa Yasuyuki, Azuma Masayuki, Tachibana Taro
Department of Bioengineering, Graduate School of Engineering, Osaka City University, Osaka, Japan.
Monoclon Antib Immunodiagn Immunother. 2013 Apr;32(2):119-24. doi: 10.1089/mab.2012.0105.
Modification of histone plays a critical role in the epigenetic regulation of gene expression. However, unlike the widely studied roles of histone methylation or acetylation of histone H3, relatively little is known about the molecular mechanisms involved in translating histone phosphorylation into a specific outcome. The present study reports on the development of antibodies (MAbs) directed against phosphorylated histone H3 (S10, T11, S28, S31, and T32), produced by the hybridization of mouse myeloma cells with lymph node cells from an immunized rat or mouse. The MAbs produced specifically recognize different sites of phosphorylation on histone H3. All of these MAbs are suitable for immunoblotting and immunofluorescence analysis. We believe that these antibodies should significantly facilitate our efforts to investigate epigenetic regulation.
组蛋白修饰在基因表达的表观遗传调控中起着关键作用。然而，与对组蛋白H3甲基化或乙酰化的广泛研究不同，对于将组蛋白磷酸化转化为特定结果所涉及的分子机制知之甚少。本研究报道了针对磷酸化组蛋白H3（S10、T11、S28、S31和T32）产生的抗体（单克隆抗体）的研发，这些抗体是通过小鼠骨髓瘤细胞与来自免疫大鼠或小鼠的淋巴结细胞杂交产生的。所产生的单克隆抗体能特异性识别组蛋白H3上不同的磷酸化位点。所有这些单克隆抗体都适用于免疫印迹和免疫荧光分析。我们相信这些抗体将极大地促进我们对表观遗传调控的研究工作。
