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TOP2A Antibody
TOP2A Antibody
- 中文名称:
- TOP2A Antibody
- 英文名称:
- TOP2A Antibody
- 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:
- AAA321238
- 规格:
- 0.1 mL|0.2 mL|2x0.2 mL|3x0.2 mL|4x0.2 mL
- 保存建议:
- 收到后,可在-20摄氏度储存12个月。
- 货期:
- 6-8周
- 来源宿主:
- Rabbit
- 反应种属:
- Human, Mouse
- 应用:
- ELISA, ICC (Immunocytochemistry), IF (Immunofluorescence), IHC (Immunohistochemistry), WB (Western 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:IgG
克隆号:N/A
特异性:TOP2A antibody detects endogenous levels of TOP2A
纯度:The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin.
形式:Liquid
Phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
浓度:1mg/ml
- 说明书:
Function: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes. May play a role in regulating the period length of ARNTL/BMAL1 transcriptional oscillation (By similarity).
Subunit Structure: Homodimer. Interacts with COPS5. Interacts with RECQL5; this stimulates DNA decatenation. Interacts with SETMAR; stimulates the topoisomerase activity (PubMed:18790802, PubMed:20457750). Interacts with DHX9; this interaction occurs in a E2 enzyme UBE2I-and RNA-dependent manner, negatively regulates DHX9-mediated double-stranded DNA and RNA duplex helicase activity and stimulates TOP2A-mediated supercoiled DNA relaxation activity (PubMed:12711669). Interacts with HNRNPU (via C-terminus); this interaction protects the topoisomerase TOP2A from degradation and positively regulates the relaxation of supercoiled DNA in a RNA-dependent manner (By similarity).
Post-translational Modifications: Phosphorylation has no effect on catalytic activity. However, phosphorylation at Ser-1106 by CSNK1D/CK1 promotes DNA cleavable complex formation.
Similarity: The N-terminus has several structural domains; the ATPase domain (about residues 1-265), the transducer domain (about 266-428) and the toprim domain (455-572) (PubMed:25202966). Comparing different structures shows ATP hydrolysis induces domain shifts in the N-terminus that are probably part of the mechanism of DNA cleavage and rejoining (PubMed:25202966). Belongs to the type II topoisomerase family.