Skip to Content
Merck
CN

05-636-I

Sigma-Aldrich

Anti-phospho-Histone H2A.X (Ser139) Antibody, clone JBW301

clone JBW301, from mouse

Synonym(s):

Anti-phospho-Histone H2A.X (Ser139) Antibody, 05-636-I | Sigma-Aldrich

Sign Into View Organizational & Contract Pricing

Select a Size

About This Item

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

Key Documents

View All Documentation
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

biological source

mouse

Quality Level

100

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

JBW301, monoclonal

species reactivity

human, rat, mouse

technique(s)

ChIP: suitable
immunocytochemistry: suitable
immunofluorescence: suitable
western blot: suitable

isotype

IgG1κ

NCBI accession no.

NP_002096

UniProt accession no.

P16104

shipped in

wet ice

target post-translational modification

phosphorylation (pSer139)

Gene Information

human ... H2AX(3014)
mouse ... H2Ax(15270)
rat ... H2Ax(500987)

General description

The histone H2A.X protein is a variant member of the H2A family of histones that is distinguished from other H2A histones by a unique carboxy-terminal sequence. This unique sequence is highly conserved throughout eukaryotic evolution and is rapidly phosphorylated by ATM or ATR at the fourth residue from the carboxy-terminus (Serine 139 in mammalian H2A.X) in response to DNA double-strand breaks (DSBs). Phosphorylation of H2A.X is important in the formation of a stable repair complex at the site of DNA damage.
H2A.X phosphorylation is a very rapid response to DNA damage, occurring within as little as one minute after exposure to ionizing radiation. Phosphorylation of H2A.X occurs irrespective of the cause of the DNA DSBs and phospho-H2A.X has been observed in response to environmental stresses that result in DSBs as well as programmed cellular events, including DNA rearrangement and apoptosis.
~17 kDa observed. Uncharacterized band(s) may appear in some lysates.

Immunogen

KLH-conjugated linear peptide corresponding to human phospho-Histone H2A. X (Ser139).

Application

Anti-phospho-Histone H2A.X (Ser139) Antibody, clone JBW301 is a highly specific mouse monoclonal antibody, that targets Histone H2A.X & has been tested in western blotting, ICC, ChIP & Immunofluorescence.
Immunocytochemistry Analysis: A 1:50-250 dilution from a representative lot detected phospho-Histone H2A. X (Ser139) in HeLa and A431 cells.
Previous lot has been demonstrated to work in Immunofluorescence and Chromatin Immunoprecipitation: See reference (Meier, Andreas et al., 2007)
Western Blotting Analysis: 0.05-1 μg/mL of this lot detected phosphorylated histone H2A.X (Ser139) in acid extracted histone lysates from Jurkat cells treated with 0.5 μM staurosporine (Catalog # 19-123).
Immunocytochemistry: 2 μg/mL of a previous lot of antibody detected phosphorylated histone H2A.X in HeLa cells treated with 0.5μM staurosporine for 4-6 hours.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Histones

Physical form

Format: Purified
Protein G Purified
Purified mouse monoclonal IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Preparation Note

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

Analysis Note

Evaluated by Western Blotting in HeLa cell lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected phospho-Histone H2A. X (Ser139) in 200 µg in staurosporine treated HeLa cells.

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.

Not finding the right product?  

Try our Product Selector Tool.

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Hong Zhang et al.
Oncology letters, 14(5), 5839-5844 (2017-11-09)
Breast cancer 1 (BRCA1) is one of the most common tumor suppressor genes in breast cancer. The BRCT domain of BRCA1 has been shown to have a critical role in tumor suppression. In a previous study, two de novo BRCT
Kranti A Mapuskar et al.
Cancer research, 77(18), 5054-5067 (2017-08-03)
Elderly cancer patients treated with ionizing radiation (IR) or chemotherapy experience more frequent and greater normal tissue toxicity relative to younger patients. The current study demonstrates that exponentially growing fibroblasts from elderly (old) male donor subjects (70, 72, and 78
Qianlan Xu et al.
Protein & cell, 7(4), 236-249 (2016-03-24)
Meiotic recombination is carried out through a specialized pathway for the formation and repair of DNA double-strand breaks (DSBs) made by the Spo11 protein. The present study shed light on the functional role of cyclin, CYC2, in Tetrahymena thermophila which
Alex W Klattenhoff et al.
Oncotarget, 8(68), 112942-112958 (2018-01-20)
DNA endonuclease eight-like glycosylase 3 (NEIL3) is one of the DNA glycosylases that removes oxidized DNA base lesions from single-stranded DNA (ssDNA) and non-B DNA structures. Approximately seven percent of human tumors have an altered NEIL3 gene. However, the role
Lucas R Smith et al.
Molecular biology of the cell, 30(16), 1985-1999 (2019-06-13)
Tissue regeneration at an injured site depends on proliferation, migration, and differentiation of resident stem or progenitor cells, but solid tissues are often sufficiently dense and constricting that nuclei are highly stressed by migration. In this study, constricted migration of
View All Related Papers

Related Content

New Products Flyer- Feb 2014 - Vol 1

"Apoptosis & Autophagy in Cancer: Cell Survival by Eluding Cell Death The ability of tumor cells to elude programmed cell death, also known as apoptosis, is a hallmark of most types of cancer. Similary, autophagy is a highly regulated, homeostatic degradative process where cells destroy their own components via the lysosomal machinery and recycle them for prolonged cell survival. Via extensive crosstalk with pro-apoptotic signaling pathways, autophagy can also contribute to cell death and greatly influence general cell health. Elucidating the correlation between autophagy and apoptotic cell death has become the focus of a great deal of research, particularly in tumor biology. On one hand, autophagy may induce cell death by degrading essential components; on the other hand, it may facilitate survival of cancer cells under unfavorable metabolic conditions."

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service