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>   首页   >   产品   >   一抗   >   精选抗体   >   磷酸化抗体   >   Anti-Histone H4 (Tyr-72), Phosphospecific Antibody   

Anti-Histone H4 (Tyr-72), Phosphospecific Antibody

     
  • 1 - Anti-Histone H4 (Tyr-72), Phosphospecific Antibody AN1812
    Western blot image of human PC3 cells untreated (lanes 1 & 3) or treated with alkaline phosphatase to dephosphorylate histone H4 (lanes 2 and 4). The blot was probed with rabbit polyclonals anti-Histone H4 (lanes 1 & 2) and anti-Histone H4 (Tyr-72) phospho-specific antibody (lanes 3 & 4).
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB
Primary Accession P62805
Reactivity Rat
Host Rabbit
Clonality Rabbit Polyclonal
Isotype IgG
Calculated MW 11367 Da
Additional Information
Gene ID 121504;554313;8294;8359;8360;8361;8362;8363;8364;8365;8366;8367;8368;8370
Other Names Hist1H4 Histone H4
Target/Specificity Chromatin structure is regulated through the activity of core histones (H2A, H2B, H3, and H4) that form the nucleosome. Histone activity is regulated by a variety of post-translational modifications, including acetylation, phosphorylation, and methylation. Histone acetylation and methylation occur primarily at lysine (K) residues in the amino-terminal tail domain. These modifications are important for the regulation of histone deposition, transcriptional activation, DNA replication and repair. Acetylation and methylation of specific lysine residues creates docking sites for DNA repair, transcription, and chromatin regulatory proteins. Methylation of histones may be regulated by phosphorylation events at sites downstream of the N-terminal tail. In histone H4, both EGFR activation and inonizing radiation induce EGFR nuclear translocation and Histone H4 (Tyr-72) phosphorylation, which creates a docking site for Set8 methyltransferase. This promotes K20 methylation in Histone H4 leading to DNA synthesis and repair.
Dilution WB~~1:1000
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsAnti-Histone H4 (Tyr-72), Phosphospecific Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
ShippingBlue Ice
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

Chromatin structure is regulated through the activity of core histones (H2A, H2B, H3, and H4) that form the nucleosome. Histone activity is regulated by a variety of post-translational modifications, including acetylation, phosphorylation, and methylation. Histone acetylation and methylation occur primarily at lysine (K) residues in the amino-terminal tail domain. These modifications are important for the regulation of histone deposition, transcriptional activation, DNA replication and repair. Acetylation and methylation of specific lysine residues creates docking sites for DNA repair, transcription, and chromatin regulatory proteins. Methylation of histones may be regulated by phosphorylation events at sites downstream of the N-terminal tail. In histone H4, both EGFR activation and inonizing radiation induce EGFR nuclear translocation and Histone H4 (Tyr-72) phosphorylation, which creates a docking site for Set8 methyltransferase. This promotes K20 methylation in Histone H4 leading to DNA synthesis and repair.

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