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Key Documents

07-745-I

Sigma-Aldrich

Anti-phospho Histone H2A (Ser129) Antibody

from rabbit, purified by affinity chromatography

Synonym(s):

Histone H2A.1

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

yeast

technique(s)

dot blot: suitable
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
inhibition assay: suitable (peptide)
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

phosphorylation (pSer129)

Gene Information

Saccharomyces cerevisiae ... Hta1(851811)

General description

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.

Specificity

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

Immunogen

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

Application

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

Quality

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.

Target description

~16 kDa observed

Physical form

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

Storage and Stability

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

Other Notes

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

Disclaimer

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.

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Robert Jordan Price et al.
mBio, 10(4) (2019-07-25)
Eukaryotic genomes are packaged into chromatin structures that play pivotal roles in regulating all DNA-associated processes. Histone posttranslational modifications modulate chromatin structure and function, leading to rapid regulation of gene expression and genome stability, key steps in environmental adaptation. Candida
Chi Kwan Tsang et al.
Molecular cell, 70(3), 502-515 (2018-05-05)
Nutrients are not only organic compounds fueling bioenergetics and biosynthesis, but also key chemical signals controlling growth and metabolism. Nutrients enormously impact the production of reactive oxygen species (ROS), which play essential roles in normal physiology and diseases. How nutrient signaling
Ryan M Hull et al.
PLoS biology, 15(6), e2001333-e2001333 (2017-06-28)
Copy number variation (CNV) is rife in eukaryotic genomes and has been implicated in many human disorders, particularly cancer, in which CNV promotes both tumorigenesis and chemotherapy resistance. CNVs are considered random mutations but often arise through replication defects; transcription

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