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     Western blot analysis of Phosphorylation of H2A.X at Serine 139 in 3T3 or Hydroxyureatreated 3T3 lysates using Phospho-Histone H2A.X (Ser139) antibody.    

  
  

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     Immunofluorescence analysis of Phospho-Histone H2A.X (Ser139) in 3T3 or Hydroxyureatreated 3T3 using Phospho-Histone H2A.X (Ser139) antibody.    

  
  

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     Immunofluorescence analysis of Phospho-Histone H2A.X (Ser139) in A549(upper, untreated or Hydroxyureatreated) and Hela(lower, untreated or Hydroxyureatreated) using Phospho-Histone H2A.X (Ser139) antibody.    

  
  

Phospho-Histone H2A.X (Ser139) antibody detects the phosphorylated form of histone H2A.X at serine 139. a key biomarker of DNA double-strand breaks (DSBs). Histone H2A.X, a variant of the H2A histone family, becomes rapidly phosphorylated at Ser139 (forming γH2A.X) in response to DNA damage, particularly DSBs induced by ionizing radiation, chemotherapeutic agents, or oxidative stress. This phosphorylation event is mediated by kinases such as ATM, ATR, and DNA-PK, which are activated as part of the DNA damage response (DDR) signaling cascade. The formation of γH2A.X foci serves as a molecular beacon, recruiting repair proteins (e.g., MDC1. 53BP1) to facilitate DNA repair and maintain genomic stability.

The Phospho-Histone H2A.X (Ser139) antibody is widely used in research to visualize and quantify DSBs, assess genomic instability, and study DDR mechanisms. Applications include immunofluorescence, Western blotting, and flow cytometry, enabling insights into cancer biology, radiation therapy, and genotoxic drug development. It is also employed in studying apoptosis, replication stress, and cellular senescence. Validating antibody specificity is critical, as non-specific signals may arise from cross-reactivity or experimental conditions. Overall, this antibody is a cornerstone tool for understanding DNA damage-related pathways and their implications in disease and therapy.