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H2A Histone Family, Member X (H2AFX) (C-Term) antibody

Details for Product No. ABIN966245, Supplier: Log in to see
Antigen
  • AW228881
  • gammaH2ax
  • h2a
  • h2a.x
  • H2A.X
  • h2a/x
  • H2A/X
  • h2afx
  • h2ax
  • H2AX
  • H2ax
  • Hist5-2ax
  • RGD1566119
  • zgc:56329
Alternatives
anti-Human H2A Histone Family, Member X antibody for Immunofluorescence
Epitope
C-Term
86
53
15
15
13
13
13
12
8
6
4
4
3
3
3
3
3
3
2
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Human
301
102
88
5
4
2
2
2
2
2
1
1
1
1
1
1
1
Host
Rabbit
256
47
1
1
Clonality
Polyclonal
Conjugate
Un-conjugated
10
10
7
6
5
5
3
2
2
2
2
2
2
2
2
1
1
1
Application
Immunohistochemistry (IHC)
227
83
81
66
43
25
23
20
14
6
5
4
2
2
2
2
2
2
1
1
1
Supplier
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Immunogen Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to Cterminal residues of human H2AFX (Histone H2A.x )
Alternative Name H2AFX (H2AFX Antibody Abstract)
Background 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).
Pathways Telomere Maintenance, DNA Damage Repair
Restrictions For Research Use only
Product cited in: Stiff, ODriscoll, Rief, Iwabuchi, Löbrich, Jeggo: "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

Lukas, Melander, Stucki, Falck, Bekker-Jensen, Goldberg, Lerenthal, Jackson, Bartek, Lukas: "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

Ward, Minn, Jorda, Chen: "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

Furuta, Takemura, Liao, Aune, Redon, Sedelnikova, Pilch, Rogakou, Celeste, Chen, Nussenzweig, Aladjem, Bonner, Pommier: "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

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

Rogakou, Boon, Redon, Bonner: "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

Background publications Stewart, Wang, Bignell, Taylor, Elledge: "MDC1 is a mediator of the mammalian DNA damage checkpoint." in: Nature, Vol. 421, Issue 6926, pp. 961-6, 2003

Rogakou, Pilch, Orr, Ivanova, Bonner: "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