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H2A Histone Family, Member X (H2AFX) (C-Term,pTyr143) antibody
|Synonyms||H2AX, H2A.X, H2A/X, H2ax, AW228881, Hist5-2ax, h2afx, MGC82078|
Alternatives Immunohistochemistry (IHC)
|8 references available|
|Price||452.38 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 5 to 7 Business Days|
|Immunogen||Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to3 C-terminal residues of human H2AFX (Histone H2A.x )|
|Description||H2AFX (Histone H2A.x ) 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. H2AFX (Histone H2A.x ) is 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. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. H2AFX interacts with numerous proteins required for DNA damage signaling and repair when phosphorylated on Ser-140. These include MDC1, TP53BP1, BRCA1 and the MRN complex, composed of MRE11A, RAD50, and NBN. Interaction with the MRN complex is mediated at least in part by NBN. Also interacts with DHX9/NDHII when phosphorylated on Ser-140. Phosphorylation at Tyr-143 (H2AXY142ph) by BAZ1B/WSTF determines the relative recruitment of either DNA repair or pro-apoptotic factors. Phosphorylation at Tyr-143 (H2AXY142ph) favors the recruitment of APBB1/FE65 and pro-apoptosis factors such as MAPK8/JNK1, triggering apoptosis. In contrast, dephosphorylation of Tyr-143 by EYA proteins (EYA1, EYA2, EYA3 or EYA4) favors the recruitment of MDC1-containing DNA repair complexes to the tail of phosphorylated Ser-140 (H2AX139ph).|
Rogakou, Pilch, Orr et al.: "DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139." in: The Journal of biological chemistry, Vol. 273, Issue 10, pp. 5858-68, 1998 (PubMed).
Rogakou, Boon, Redon et al.: "Megabase chromatin domains involved in DNA double-strand breaks in vivo." in: The Journal of cell biology, Vol. 146, Issue 5, pp. 905-16, 1999 (PubMed).
Ward, Chen: "Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress." in: The Journal of biological chemistry, Vol. 276, Issue 51, pp. 47759-62, 2001 (PubMed).
Stewart, Wang, Bignell et al.: "MDC1 is a mediator of the mammalian DNA damage checkpoint." in: Nature, Vol. 421, Issue 6926, pp. 961-6, 2003 (PubMed).
Furuta, Takemura, Liao et al.: "Phosphorylation of histone H2AX and activation of Mre11, Rad50, and Nbs1 in response to replication-dependent DNA double-strand breaks induced by mammalian DNA topoisomerase I cleavage complexes." in: The Journal of biological chemistry, Vol. 278, Issue 22, pp. 20303-12, 2003 (PubMed).
Ward, Minn, Jorda et al.: "Accumulation of checkpoint protein 53BP1 at DNA breaks involves its binding to phosphorylated histone H2AX." in: The Journal of biological chemistry, Vol. 278, Issue 22, pp. 19579-82, 2003 (PubMed).
Stiff, ODriscoll, Rief et al.: "ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation." in: Cancer research, Vol. 64, Issue 7, pp. 2390-6, 2004 (PubMed).
Lukas, Melander, Stucki et al.: "Mdc1 couples DNA double-strand break recognition by Nbs1 with its H2AX-dependent chromatin retention." in: The EMBO journal, Vol. 23, Issue 13, pp. 2674-83, 2004 (PubMed).