Anti-phospho Histone H2A (Ser129) Antibody

Evaluated by Western Blotting in untreated and Methyl methanesulfonate (MMS) treated yeast nuclear extract.

Western Blotting Analysis: 0.02 µg/mL of this antibody detected an increase in signal for phospho Histone H2A (Ser129) in MMS treated yeast nuclear extract over untreated yeast nuclear extract.

Detect Histone H2A using this rabbit polyclonal antibody, Anti-phospho Histone H2A (Ser129) Antibody validated for use in western blotting, Dot Blot, Peptide Inhibition Assay, IP & ICC.

Dot Blot (Specificity) Analysis: 0.05 µg/mL from a representative lot detected phospho Histone H2A (Ser129) in various panels of modified and non-modified Histones.

Immunoprecipitation Analysis: A 1:100 dilution from a represenetative lot immunoprecipitated phospho Histone H2A (Ser129) from yeast extracts.

Immunohistochemistry Analysis: A 1:1,000 dilution from a lot detected phospho Histone H2A (Ser129) from yeast cells.

Research Category
Epigenetics & Nuclear Function

Research Sub Category
Histones

This antibody is specifically recognizes yeast phospho-Histone H2A (Ser129)

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Histone H2A is one of the 5 main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N terminal tail H2A is involved with the structure of the nucleosomes of the ′beads on a string′ structure. Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. Histones are modified post-translationally by acetylation, phosphorylation, methylation, and ubiquitination and these modifications regulate DNA transcription, repair, recombination, and replication. Ubiquitylation usually targets the substrate for degradation, although histones H2A and H2B are actually stabilized by a single ubiquitin conjugation. Histone ubiquitination has been correlated with DNA repair and transcription, cellular differentiation, cell cycle regulation, spermatogenesis, protein trafficking, and response to stress. Histone H2A is one of four components of the core nucleosomal structure. The nucleosome represents a unit of chromatin in which DNA is wrapped around a histone octamer. Histones undergo a number of post-translational modifications (PTM) in response to various stimuli that may induce changes in the structure of the nucleosome and hide or expose DNA sequences. Histone H2A, in particular, undergoes acetylation on lysine 5 by the Tip60 enzyme which may promote unfolding of chromatin and transcription. In addition, H2A is phosphorylated on serine 1 and serine 139 (H2A.X) residues which mark mitosis and gene repression, and DNA damage, respectively. Gene repression may also result from the sumoylation of H2A’s lysine 126 residue. In addition, ubiquitination of the H2A lysine 119 residue may play a role in spermatogenesis. It is the pattern of different modifications on several histone residues that alter chromatin, rather than modification of single residues.

~16 kDa observed

KLH-conjugated linear peptide corresponding to the C-terminus of yeast Histone H2A phosphorylated at Ser129.

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Affinity purified

Purified rabbit in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.