Licensed to Novus Biologicals LLC under U.S. Patent Nos. 6,362,317 and 6,884,873.
Immunogen
This Histone H2AX [p Ser139] Antibody (9F3) was developed against a synthetic phospho-peptide derived from the sequence of human Histone H2AX phosphorylated at Ser139.
Modification
p Ser139
Marker
DNA Double-strand break marker
Specificity
Specific to the portion of Human Histone H2AX phosphorylated at Ser139.
Isotype
IgG1 Kappa
Clonality
Monoclonal
Host
Mouse
Gene
H2AX
Purity
Protein G purified
Innovator's Reward
Test in a species/application not listed above to receive a full credit towards a future purchase.
Use in Immunocytochemistry reported in scientific literature (PMID:33088425).
Theoretical MW
15 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using NBP1-19255 in the following applications:
Please note that this antibody is reactive to Mouse and derived from the same host, Mouse. Mouse-On-Mouse blocking reagent may be needed for IHC and ICC experiments to reduce high background signal. You can find these reagents under catalog numbers PK-2200-NB and MP-2400-NB. Please contact Technical Support if you have any questions.
Packaging, Storage & Formulations
Storage
Store at -20C. Avoid freeze-thaw cycles.
Buffer
PBS (pH 7.2) and 50% Glycerol
Preservative
0.09% Sodium Azide
Purity
Protein G purified
Alternate Names for Histone H2AX [p Ser139] Antibody (9F3)
H2A.X
H2A/X
H2AFX
Histone H2AX
Background
Gamma H2AX (gammaH2AX) is the phosphorylated version of histone H2AX and is a marker for double-stranded breaks (DSBs) caused by DNA damage (1-4). H2AX is a variant of histone H2A, one of the histone core molecules forming the nucleosome, and is a vital component in repairing DNA damage (1-4). The H2AX variant represents between 2-25% of total H2A (1-3). Human H2AX protein is 143 amino acids in length and has a theoretical molecular weight of 15 kDa (5). As a result of DSBs, H2AX becomes phosphorylated at serine-139 and gamma H2AX is generated as a response to genomic instability (1-4). Gamma H2AX and its phosphorylation can be detected through western blotting and immunofluorescence, serving as a biomarker for DSB frequency (1-4). Ataxia telangiectasia mutated (ATM) is considered a key protein for H2AX phosphorylation (1-4). Upon the phosphorylation and formation of gamma H2AX, many repair proteins become associated including breast cancer 1 protein (BRCA1), NBS1 (Nijmegen breakage syndrome 1)/hMRE11 (human meiotic recombination 11 protein)/ hRAD50 (N/M/R) repair complex, and 53BP1 (p53 binding protein 1) (1-4). Gamma H2AX detection assays are currently utilized for a variety of purposes, from studying DNA repair to drug development and radiation biodosimetry (4).
References
1. Palla, V. V., Karaolanis, G., Katafigiotis, I., Anastasiou, I., Patapis, P., Dimitroulis, D., & Perrea, D. (2017). gamma-H2AX: Can it be established as a classical cancer prognostic factor?. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine. https://doi.org/10.1177/1010428317695931
2. Kuo, L. J., & Yang, L. X. (2008). Gamma-H2AX - a novel biomarker for DNA double-strand breaks. In vivo (Athens, Greece).
3. Kinner, A., Wu, W., Staudt, C., & Iliakis, G. (2008). Gamma-H2AX in recognition and signaling of DNA double-strand breaks in the context of chromatin. Nucleic acids research. https://doi.org/10.1093/nar/gkn550
4. Redon, C. E., Weyemi, U., Parekh, P. R., Huang, D., Burrell, A. S., & Bonner, W. M. (2012). gamma-H2AX and other histone post-translational modifications in the clinic. Biochimica et biophysica acta. https://doi.org/10.1016/j.bbagrm.2012.02.021
5. H2AX: Uniprot (P16104)
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
Yang J, Griffin P, Vera D et al. Erosion of the Epigenetic Landscape and Loss of Cellular Identity as a Cause of Aging in Mammals SSRN Journal 2019-10-03 (ICC/IF, Mouse)
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