SHOPPING BASKET: 0 item(s) - £0.00  

You have no items in your shopping cart.

Anti-Histone H2A.X (Phospho-Ser139) antibody

[STJ97186] Download PDF Print Data Sheet

* Required Fields

£0.00
Product name Anti-Histone H2A.X (Phospho-Ser139) antibody
Short Description Rabbit Polyclonal to Histone H2A.X (Phospho-Ser139).
Description Histone H2A.X is a protein encoded by the H2AFX gene which is approximately 15,1 kDa. Histone H2A.X is localised to the nucleus. It is involved in DNA double-strand break repair and mitotic cell cycle. Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units. Histone H2A.X is expressed in the lung, nervous system, intestine, skin and eye. Mutations in the H2AFX gene may result in Nijmegen breakage syndrome and ataxia-telangiectasia. STJ97186 was affinity-purified from rabbit antiserum by affinity-chromatography using specific immunogen. This antibody detects endogenous Histone H2A.X (PhosphoSer139) protein.
Applications WB
Dilution range WB 1:1000-2000
Specificity The antibody detects endogenous Histone H2A.X (PhosphoSer139) protein.
Protein Name Histone H2AX
H2a/x
Histone H2A.X
Immunogen Synthetic Peptide
Storage Instruction Store at -20°C, and avoid repeat freeze-thaw cycles.
Note For Research Use Only (RUO).
Host Rabbit
Clonality Polyclonal
Reactivity Human, Mouse, Rat
Conjugation Unconjugated
Purification The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using specific immunogen.
Isotype IgG
Formulation Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Gene ID 3014
Gene Symbol H2AFX
Database Links HGNC:4739
OMIM:601772
Alternative Names H2AFX antibody
H2AX antibody
Histone H2AX antibody
H2a/x antibody
Histone H2A.X antibody
Histone H2A.X (Phospho-Ser139) antibody
Function Variant histone H2A which 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. 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.
Post-translational Modifications Phosphorylated on Ser-140 (to form gamma-H2AX or H2AX139ph) in response to DNA double strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks, and may also occur during meiotic recombination events and immunoglobulin class switching in lymphocytes. Phosphorylation can extend up to several thousand nucleosomes from the actual site of the DSB and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Widespread phosphorylation may also serve to amplify the damage signal or aid repair of persistent lesions. Phosphorylation of Ser-140 (H2AX139ph) in response to ionizing radiation is mediated by both ATM and PRKDC while defects in DNA replication induce Ser-140 phosphorylation (H2AX139ph) subsequent to activation of ATR and PRKDC. Dephosphorylation of Ser-140 by PP2A is required for DNA DSB repair. In meiosis, Ser-140 phosphorylation (H2AX139ph) may occur at synaptonemal complexes during leptotene as an ATM-dependent response to the formation of programmed DSBs by SPO11. Ser-140 phosphorylation (H2AX139ph) may subsequently occurs at unsynapsed regions of both autosomes and the XY bivalent during zygotene, downstream of ATR and BRCA1 activation. Ser-140 phosphorylation (H2AX139ph) may also be required for transcriptional repression of unsynapsed chromatin and meiotic sex chromosome inactivation (MSCI), whereby the X and Y chromosomes condense in pachytene to form the heterochromatic XY-body. During immunoglobulin class switch recombination in lymphocytes, Ser-140 phosphorylation (H2AX139ph) may occur at sites of DNA-recombination subsequent to activation of the activation-induced cytidine deaminase AICDA. 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). ; Monoubiquitination of Lys-120 (H2AXK119ub) by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression (By similarity). Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events. ; Acetylation at Lys-37 increases in S and G2 phases. This modification has been proposed to play a role in DNA double-strand break repair (By similarity).
Cellular Localization Nucleus Chromosome
Sequence and Domain Family The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.

Tags:

Use spaces to separate tags. Use single quotes (') for phrases.

Bad Good
Enter the code in the box below: