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Histone H2AT120ph antibody (pAb)
Histone H2AT120ph antibody (pAb)
- 中文名称：
- Histone H2AT120ph antibody (pAb)
- 英文名称：
- Histone H2AT120ph antibody (pAb)
- 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：
- AAA59871
- 规格：
- 0.01 mL|0.1 mL|2x0.1 mL|3x0.1 mL|4x0.1 mL
- 保存建议：
- Some products may be shipped at room temperature. This will not affect their stability or performance. Avoid repeated freeze/thaw cycles by aliquoting items into single-use fractions for storage at -20°C for up to 2 years. Keep all reagents on ice when not in storage.1ug/ul
- 货期：
- 6-8周
- 来源宿主：
- Rabbit
- 反应种属：
- Human, Wide Range Predicted
- 应用：
- WB (Western Blot), DB (Dot Blot)
- 免责声明：
- *本产品仅供科研实验使用，不得用于临床诊断。*
- 其他：
克隆性:Polyclonal
同型:Serum
克隆号:N/A
特异性:N/A
纯度:N/A
形式：Rabbit serum containing 30% glycerol and 0.035% sodium azide. Sodium azide is highly toxic. For your convenience, an IgG version of this antibody that was purified by Protein A Chromatography is also available.
浓度：N/A
- 说明书：
Background: Histone H2A is one of the core components of the nucleosome. The nucleosome is the smallest subunit of chromatin and consists of 147 base pairs of DNA wrapped around an octamer of core histone proteins (two each of Histone H2A, Histone H2B, Histone H3 and Histone H4). Histone H1 is a linker histone, present at the interface between the nucleosome core and DNA entry/exit points; it is responsible for establishing higher-order chromatin structure. Chromatin is subject to a variety of chemical modifications, including post-translational modifications of the histone proteins and the methylation of cytosine residues in the DNA. Reported histone modifications include acetylation, methylation, phosphorylation, ubiquitylation, glycosylation, ADP-ribosylation, carbonylation and SUMOylation; they play a major role in regulating gene expression. Phosphorylation of histones occurs at multiple sites during mitosis. H2A Thr120 phosphorylation is observed on chromatin during both mitosis and meiosis. Thr120 phosphorylation is inversely correlated with ubiquitylation of H2A Lys119 in meiotic mouse spermatocytes. In Drosophila, loss of H2A Thr120 phosphorylation is associated with a failure to disassemble the synaptonemal complex, impaired loading of condensin and female infertility. It is possible that H2A Thr120 phosphorylation is involved in the regulation of chromatin structure.
