Phospho-Histone H2A (Ser129) Antibody [A4N9]

Application: Reactivity: Human, Saccharomyces cerevisiae

Lane 1: Saccharomyces cerevisiae (0.2% Methyl methanesulfonate, 1 h), Lane 2: Saccharomyces cerevisiae

Usage Information

Dilution
WB1:5000 CHIP1:500

Application
WB, ChIP, ELISA

Reactivity
Human, Saccharomyces cerevisiae

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
14 kDa 14 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
Phospho-Histone H2A (Ser129) Antibody [A4N9] detects endogenous levels of total Histone H2A protein only when it is phosphorylated at Ser129.

Clone
A4N9

Synonym(s)
H2A2; YBL003C; YBL0103; HTA2; Histone H2A.2

Background
Phospho Histone H2A at Ser129 (H2A S129ph) is a conserved, DNA damage–induced histone mark that plays a central role in the chromatin based signaling cascade coordinating double strand break (DSB) repair and genome integrity, particularly in yeast and mammalian systems where it functions as part of the broader H2A.X family of variant histones. The modification occurs at a C terminal SQ motif that is phosphorylated by phosphoinositide 3 kinase related kinases such as ATM and ATR in response to DNA breaks, generating a localized phospho epitope that spreads over kilobase scale chromatin regions flanking the lesion and thereby serving as a nucleation platform for downstream repair factors. H2A S129ph directly recruits chromatin modifying complexes such as the NuA4 histone acetyltransferase and Ino80/Swr1 type ATP dependent remodeling complexes, which are anchored through specific subunits that recognize the phosphorylated tail, thus promoting acetylation and restructuring of nearby nucleosomes to enhance accessibility of damaged DNA to repair enzymes. This phospho H2A–dependent recruitment supports efficient homologous recombination and non homologous end joining by facilitating the assembly and retention of DSB sensing and processing factors at the break site, while also interfacing with cell cycle checkpoints to delay progression until repair is complete. H2A S129ph is widely used as a sensitive, high resolution readout for DSB generation and repair efficiency, and dysregulation of its phosphorylation or recognition machinery contributes to defective repair responses, increased genomic instability, and hypersensitivity to genotoxic agents, so that H2A S129ph dependent signaling is ultimately dysregulated in DNA repair deficient and cancer prone backgrounds.

Background

Phospho Histone H2A at Ser129 (H2A S129ph) is a conserved, DNA damage–induced histone mark that plays a central role in the chromatin based signaling cascade coordinating double strand break (DSB) repair and genome integrity, particularly in yeast and mammalian systems where it functions as part of the broader H2A.X family of variant histones. The modification occurs at a C terminal SQ motif that is phosphorylated by phosphoinositide 3 kinase related kinases such as ATM and ATR in response to DNA breaks, generating a localized phospho epitope that spreads over kilobase scale chromatin regions flanking the lesion and thereby serving as a nucleation platform for downstream repair factors. H2A S129ph directly recruits chromatin modifying complexes such as the NuA4 histone acetyltransferase and Ino80/Swr1 type ATP dependent remodeling complexes, which are anchored through specific subunits that recognize the phosphorylated tail, thus promoting acetylation and restructuring of nearby nucleosomes to enhance accessibility of damaged DNA to repair enzymes. This phospho H2A–dependent recruitment supports efficient homologous recombination and non homologous end joining by facilitating the assembly and retention of DSB sensing and processing factors at the break site, while also interfacing with cell cycle checkpoints to delay progression until repair is complete. H2A S129ph is widely used as a sensitive, high resolution readout for DSB generation and repair efficiency, and dysregulation of its phosphorylation or recognition machinery contributes to defective repair responses, increased genomic instability, and hypersensitivity to genotoxic agents, so that H2A S129ph dependent signaling is ultimately dysregulated in DNA repair deficient and cancer prone backgrounds.

References
https://pubmed.ncbi.nlm.nih.gov/15610740/ https://pubmed.ncbi.nlm.nih.gov/17353265/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%