The antibody detects endogenous level of Histone H2A.X only when phosphorylated at serine 139.
Purification
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography usingepitope-specific phosphopeptide. The antibody against non-phosphopeptide was removedby chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Immunogen
Peptide sequence around phosphorylation site of pSer139 (Q-A-S (p) -Q-E) derived from Human Histone H2A.X. Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates.
H2AFX
Reactivity: Human
IHC, ELISA
Host: Rabbit
Polyclonal
unconjugated
Application Notes
Western blotting: 1:500-1:1000 Immunofluorescence: 1:100-1:200
Restrictions
For Research Use only
Format
Liquid
Concentration
1 mg/mL
Buffer
Phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150 mM NaCl, 0.02 % sodium azide and 50 % glycerol.
Preservative
Sodium azide
Precaution of Use
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C/-20 °C
Storage Comment
Store at -20 °C for long term preservation (recommended). Store at 4 °C for short term use.
Cui, Zhang, Du, Wang, Archacki, Zhang, Yuan, Ke, Li, Li, Li, Li, Tang, Yin, Liu: "HSF4 is involved in DNA damage repair through regulation of Rad51." in: Biochimica et biophysica acta, Vol. 1822, Issue 8, pp. 1308-15, (2012) (PubMed).
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Background
Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation.