Anti-Phospho-Histone-H2A.X (Ser139) pAb

  • Applications
    • IF
    • WB
  • Target H2A.X
  • Host Species Rabbit
  • Species Reactivities Human, Mouse, Rat
  • Code # CY-P1015
  • Size 25 μg
  • Price


The histone H2A.X protein is a variant member of the H2A family of histones and is distinguished from other H2A histones by a unique carboxy-terminal sequence. This unique sequence is highly conserved throughout eukaryotic evolution and is rapidly phosphorylated at the fourth residue from the carboxy-terminus (Ser139 in mammalian H2A.X) in response to DNA double-strand breaks (DSBs). H2A.X phosphorylation is a very rapid response to DNA damage, occurring within as little as one minute after exposure to ionizing radiation. Phosphorylation of H2A.X occurs irrespective of the cause of the DNA DSBs and phospho-H2A.X has been observed in response to environmental stresses that result in DSBs as well as programmed cellular events, including DNA rearrangement and apoptosis.
  • Antibody Type:
  • Application:
    IF, WB
  • Concentration:
    0.5 mg/mL
  • Conjugate:
  • Description:

    Polyclonal Antibody of 25 μg targeting H2A.X for IF, WB.

  • Formulation:
    Supplied in 20mM phosphatase buffer (pH 7.5), 300mM NaCl, 50% glycerol.
  • Host Species:
  • Immunogen:
    Near the Ser139 phosphorylated peptide synthesis of human Histone H2A.X. (binding KLH)
  • Isotype:
  • Product Type:
  • Reactivity:
    Phospho-Histone H2A.X Ser139 Antibody detects the ~14 kDa endogenous Histone H2A.X only when phosphorylated at serine139. The antibody does not recognize the unphosphorylated protein, nor does it recognize other histones.
  • Research Area:
  • Short Description:

    Anti-Phospho-Histone-H2A.X (Ser139) Polyclonal Antibody.

  • Size:
    25 μg
  • Species Reactivity:
    Human, Mouse, Rat
  • Storage Temperature:
  • Target:
  1. Burma S, et al. ATM phosphorylates histone H2AX in response to DNA double-strand breaks. J. Biol. Chem. 276:42462-7 (2001)
  2. Bassing CH, et al. Histone H2AX: a dosagedependent suppressor of oncogenic translocations and tumors. Cell 114::359-70 (2003)
  3. Kobayashi J, et al. NBS1 localizes to gamma- H2AX foci through interaction with the FHA/BRCT domain. Curr. Biol. 12:1846-51 (2002)
  4. Celeste A, et al. Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks. Nat. Cell Biol. 5:675-9 (2003)
  5. Rogakou EP, et al. DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J. Biol. Chem. 273:5858-68 (1998).
  6. Rogakou EP, et al. Initiation of DNA fragmentation during apoptosis induces phosphorylation of H2AX histone at serine 139. J. Biol. Chem. 275:9390-5 (2000)