Anti-Histone H2A.X Antibody (pSer139)__Rabbit Anti-Human Histone H2A.X (pSer139) Polyclonal Sapitinib
Storage Buffer
PBS (without Mg2+ and Ca2+), pH 7.4, 50% glycerol, 150mM NaCl, 0.02% sodium azide
Storage Temperature
-20ºC
Shipping Temperature
Blue Ice or 4ºC
Purification
Affinity Purified
Clonality
Polyclonal
Isotype
IgG
Specificity
Detects endogenous levels of Histone H2A.X only when phosphorylated at serine 139.
Cite This Product
Rabbit Anti-Human Histone H2A.X (pSer139) Polyclonal (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SPC-1251)
Certificate of Analysis
A 1:1000 dilution of SPC-1251 was sufficient for detection of Histone H2A.X in 10 µg of 293T cell lysates by ECL immunoblot analysis using Goat Anti-Rabbit IgG:HRP as the secondary antibody.
References PubMed ID::http://www.ncbi.nlm.nih.gov/pubmed/19128510
Alternative Names
H2A histone family member X Antibody, H2A.FX Antibody, H2A.X Antibody, H2AFX Antibody, H2AX histone Antibody, Histone 2A Antibody, Histone 2AX Antibody
Research Areas
Cell Signaling, DNA Damage and Repair, DNA Damage Recognition, DNA/RNA, Epigenetics and Nuclear Signalling, Histones
Cellular Localization
Chromosome, Nucleus
Accession Number
NP_002096.1
Gene ID
3014
Swiss Prot
P16104
Scientific Background
H2AX (H2A histone family, member X) is one of several genes coding for histone H2A. H2AX becomes phosphorylated on serine 139 as a reaction on DNA Double-strand breaks (DSB). The kinases of the PI3-family (Ataxia telangiectasia mutated, ATR and DNA-PKcs) are responsible for this phosphorylation, especially ATM. The role of the phosphorylated form potentially allows for space for the recruitment of proteins necessary during repair of DSBs. In addition to its role in DNA-damage repair, H2A.X is required for DNA fragmentation during apoptosis and is phosphorylated by various kinases in response to apoptotic signals. H2A.X is phosphorylated at Ser139 by DNA-PK in response to cell death receptor activation, c-Jun N-terminal Kinase (JNK1) in response to UV-A irradiation, and p38 MAPK in response to serum starvation.
References
1. Kuo L.J., and Yang L.X. (2008) In Vivo. 22(3): 305-309.
2. Mukherjee B., et al. (2006) DNA Repair (Amst). 5: 575-90.
3. Solier S., et al. (2009) Mol Cell Biol. 29: 68-82.
4. Lu C., et al. (2006) Mol Cell. 23: 121-32.
5. Lu C., et al. (2008) FEBS Lett. 582: 2703-8.
2. Mukherjee B., et al. (2006) DNA Repair (Amst). 5: 575-90.
3. Solier S., et al. (2009) Mol Cell Biol. 29: 68-82.
4. Lu C., et al. (2006) Mol Cell. 23: 121-32.
5. Lu C., et al. (2008) FEBS Lett. 582: 2703-8.