anti-H2AFX antibody product blog
Tags: Antibody; Monoclonal Antibody; H2AFX; anti-H2AFX antibody; Histone H2A.X;
The H2AFX h2afx (Catalog #MBS6011732) is an Antibody produced from Rabbit and is intended for research purposes only. The product is available for immediate purchase. The Histone H2A.X, phosphorylated (Ser139) (H2a/x, H2AFX, H2AX) (PE) reacts with Human, Monkey, Mouse, Rat and may cross-react with other species as described in the data sheet. MyBioSource\'s Histone H2A.X can be used in a range of immunoassay formats including, but not limited to, Flow Cytometry (FC/FACS).Suitable for use in Flow Cytometry.
Dilution: Flow Cytometry: 1:50. Researchers should empirically determine the suitability of the H2AFX h2afx for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process.
The H2AFX h2afx product has the following accession number(s) (GI #4504253) (NCBI Accession #NP_002096.1) (Uniprot Accession #P16104). Researchers may be interested in using Bioinformatics databases such as those available at The National Center for Biotechnology Information (NCBI) website for more information about accession numbers and the proteins they represent. Even researchers unfamiliar with bioinformatics databases will find the NCBI databases to be quite user friendly and useful.
To buy or view more detailed product information and pricing, please click on the technical datasheet page below:
Please refer to the product datasheet for known applications of a given antibody. We\'ve tested the Histone H2A.X, phosphorylated (Ser139) (H2a/x, H2AFX, H2AX) (PE) with the following immunoassay(s):
Flow Cytometry (FC/FACS) (Flow cytometric analysis of Jurkat cells, untreated (blue) or etoposide-treated (green), using Phospho-Histone H2A.X (Ser139) Rabbit mAb (PE Conjugate).)
Histone H2A.X is a variant histone that represents approximately 10% of the total H2A histone proteins in normal human fibroblasts (1). H2A.X is required for checkpoint-mediated cell cycle arrest and DNA repair following double-stranded DNA breaks (1). DNA damage, caused by ionizing radiation, UV-light, or radiomimetic agents, results in rapid phosphorylation of H2A.X at Ser139 by PI3K-like kinases, including ATM, ATR, and DNA-PK (2,3). Within minutes following DNA damage, H2A.X is phosphorylated on Ser139 at sites of DNA damage (4). This very early event in the DNA-damage response is required for recruitment of a multitude of DNA-damage response proteins, including MDC1, NBS1, RAD50, MRE11, 53BP1, and BRCA1 (1). 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 on Ser139 by DNA-PK in response to cell death receptor activation, c-Jun N-terminal Kinase (JNK1) in response to UV-An irradiation, and p38 MAPK in response to serum starvation (5-8). H2A.X is constitutively phosphorylated on Tyr142 in undamaged cells by WSTF (Williams-Beuren syndrome transcription factor) (9,10). Upon DNA damage, and concurrent with phosphorylation of Ser139, Tyr142 is dephosphorylated at sites of DNA damage by recruited EYA1 and EYA3 phosphatases (9). While phosphorylation of Ser139 facilitates the recruitment of DNA repair proteins and apoptotic proteins to sites of DNA damage, phosphorylation of Tyr142 appears to determine which set of proteins are recruited. Phosphorylation of H2A.X on Tyr142 inhibits the recruitment of DNA repair proteins and promotes binding of pro-apoptotic factors such as JNK1 (9). Mouse embryonic fibroblasts expressing only mutant H2A.X Y142F, which favors recruitment of DNA repair proteins over apoptotic proteins, show a reduced apoptotic response to ionizing radiation (9). Thus, it appears that the balance of H2A.X Tyr142 phosphorylation and dephosphorylation provides a switch mechanism to determine cell fate after DNA damage.