Antibody data
- Antibody Data
- Antigen structure
- References [5]
- Comments [0]
- Validations [0]
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- Product number
- ABIN394195 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-H2A Histone Family, Member X (H2AFX) antibody
- Antibody type
- Monoclonal
- Description
- This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.
- Reactivity
- Human
- Host
- Mouse
- Isotype
- IgG
- Antibody clone number
- 2H5
- Vial size
- 100 μg
- Storage
- Maintain 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
Submitted references H2AX phosphorylation screen of cells from radiosensitive cancer patients reveals a novel DNA double-strand break repair cellular phenotype.
Phosphorylation of histone H2A.X by DNA-dependent protein kinase is not affected by core histone acetylation, but it alters nucleosome stability and histone H1 binding.
Acetylation of H2AX on lysine 36 plays a key role in the DNA double-strand break repair pathway.
Differences in the kinetics of gamma-H2AX fluorescence decay after exposure to low and high LET radiation.
High-resolution profiling of gammaH2AX around DNA double strand breaks in the mammalian genome.
Vasireddy RS, Sprung CN, Cempaka NL, Chao M, McKay MJ
British journal of cancer 2010 May 11;102(10):1511-8
British journal of cancer 2010 May 11;102(10):1511-8
Phosphorylation of histone H2A.X by DNA-dependent protein kinase is not affected by core histone acetylation, but it alters nucleosome stability and histone H1 binding.
Li A, Yu Y, Lee SC, Ishibashi T, Lees-Miller SP, Ausió J
The Journal of biological chemistry 2010 Jun 4;285(23):17778-88
The Journal of biological chemistry 2010 Jun 4;285(23):17778-88
Acetylation of H2AX on lysine 36 plays a key role in the DNA double-strand break repair pathway.
Jiang X, Xu Y, Price BD
FEBS letters 2010 Jul 2;584(13):2926-30
FEBS letters 2010 Jul 2;584(13):2926-30
Differences in the kinetics of gamma-H2AX fluorescence decay after exposure to low and high LET radiation.
Schmid TE, Dollinger G, Beisker W, Hable V, Greubel C, Auer S, Mittag A, Tarnok A, Friedl AA, Molls M, Röper B
International journal of radiation biology 2010 Aug;86(8):682-91
International journal of radiation biology 2010 Aug;86(8):682-91
High-resolution profiling of gammaH2AX around DNA double strand breaks in the mammalian genome.
Iacovoni JS, Caron P, Lassadi I, Nicolas E, Massip L, Trouche D, Legube G
The EMBO journal 2010 Apr 21;29(8):1446-57
The EMBO journal 2010 Apr 21;29(8):1446-57
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