05-636-AF555
Anti-phospho-H2A.X Antibody (Ser139), clone JBW301, Alexa Fluor™ 555 Conjugate
clone JBW301, from mouse, ALEXA FLUOR™ 555
Synonym(s):
H2AXS139P, Histone H2A.X (phospho S139)
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
mouse
Quality Level
conjugate
ALEXA FLUOR™ 555
antibody form
purified antibody
antibody product type
primary antibodies
clone
JBW301, monoclonal
species reactivity
human
species reactivity (predicted by homology)
vertebrates (based on 100% sequence homology)
technique(s)
immunocytochemistry: suitable
isotype
IgG1
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
phosphorylation (pSer139)
Gene Information
human ... H2AX(3014)
General description
Histone H2A.X, also known as H2A/X, or H2A.X, and encoded by the gene name H2AFX and H2AX, is a variant of histone H2A and is similarly associated with genomic DNA. However, histone is structurally different from other members of the H2A family in possessing a C-terminal tail that contains the Ser139 residue that is phosphorylated in response to breaks in double-stranded DNA. The phosphorylation of H2A.X is a rapid process that is mediated by ATM/ATR proteins. As a member of the histone H2A family, histone H2A.x (H2A.x) is a variant histone H2A which replaces conventional H2A in a subset of nucleosomes. H2A.x is involved in the DNA repair of double-strand breakage (DSB) damage on nuclear DNA. After a double strand DNA break, H2A.x is rapidly phosphorylated at serine 139 by ATM kinase and becomes gamma-H2AFX. This phosphorylation step 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 (1). As a part of posttranslational modifications during apoptosis caused by severe DNA damage, high expression of phosphorylated H2A.x is considered as an accurate indicator of apoptosis.
Immunogen
Linear peptide corresponding to phospho-Histone H2A.X (Ser139).
Application
Anti-phospho-H2A.X (Ser139), clone JBW301, Alexa Fluor™ 555 Conjugate is an antibody against phospho-H2A.X (Ser139) for use in Immunocytochemistry.
Chromatin Immunoprecipitation Analysis: A representative lot of the non-conjugated form of this antibody (Cat. # 05-636) was used to detect phospho-Histone H2A.X (Ser139) by ChIP (Meier, A. et al. (2007) EMBO J., 26:2707-18).
Western Blot Analysis: 0.05-1 μg/mL of a representative lot of the non-conjugated form of this antibody (Cat. # 05-636) detected phosphorylated histone H2A.X (Ser139) in acid extracted histone lysates from Jurkat cells treated with 0.5 μM staurosporine (Catalog # 19-123).
Western Blot Analysis: 0.05-1 μg/mL of a representative lot of the non-conjugated form of this antibody (Cat. # 05-636) detected phosphorylated histone H2A.X (Ser139) in acid extracted histone lysates from Jurkat cells treated with 0.5 μM staurosporine (Catalog # 19-123).
Research Category
Epigenetics & Nuclear Function
Epigenetics & Nuclear Function
Research Sub Category
Histones
Histones
Quality
Evaluated by Immunocytochemistry in HeLa cells +/- Staurosporin treatment.
Immunocytochemistry Analysis: A 1:100 dilution of this antibody detected phospho-Histone H2A.X (Ser139) in HeLa cells +/- Staurosporin treatment.
Immunocytochemistry Analysis: A 1:100 dilution of this antibody detected phospho-Histone H2A.X (Ser139) in HeLa cells +/- Staurosporin treatment.
Target description
17 kDa observed
Physical form
Protein G Purified
Purified mouse monoclonal IgG1 in buffer containing PBS with 15 mg/mL BSA and 0.1% azide
Storage and Stability
Stable for 1 year at 2-8°C from date of receipt.
Other Notes
Concentration: Please refer to lot specific datasheet.
Legal Information
ALEXA FLUOR is a trademark of Life Technologies
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.
WGK
WGK 2
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.
Customers Also Viewed
Andreas Meier et al.
The EMBO journal, 26(11), 2707-2718 (2007-05-12)
Phosphorylated histone H2AX (gammaH2AX) is generated in nucleosomes flanking sites of DNA double-strand breaks, triggering the recruitment of DNA-damage response proteins such as MDC1 and 53BP1. Here, we study shortened telomeres in senescent human cells. We show that most telomeres
Yujie Huang et al.
Frontiers in oncology, 11, 586771-586771 (2021-03-16)
HPV-positive (HPV+) cervical cancer cells are more radioresistant compared with HPV-negative (HPV-) cervical cancer cells, but the underlying mechanism is not fully illuminated. Our previous mass spectrometry data showed that Ras-associated binding protein Rab12 was up-regulated by HPV, and this
Miguel A Galindo-Campos et al.
Cell death and differentiation, 26(12), 2667-2681 (2019-04-19)
Poly (ADP-ribose) polymerase (PARP)-1 and PARP-2 regulate the function of various DNA-interacting proteins by transferring ADP-ribose emerging from catalytic cleavage of cellular β-NAD+. Hence, mice lacking PARP-1 or PARP-2 show DNA perturbations ranging from altered DNA integrity to impaired DNA
Panagiotis Karakaidos et al.
Bioengineering (Basel, Switzerland), 9(8) (2022-08-26)
Laser-based techniques for printing cells onto different substrates with high precision and resolution present unique opportunities for contributing to a wide range of biomedical applications, including tissue engineering. In this study, laser-induced forward transfer (LIFT) printing was employed to rapidly
Charles W Morgan et al.
Proceedings of the National Academy of Sciences of the United States of America, 112(27), 8344-8349 (2015-06-25)
Cellular demolition during apoptosis is completed by executioner caspases, that selectively cleave more than 1,500 proteins but whose individual roles are challenging to assess. Here, we used an optimized site-specific and inducible protease to examine the role of a classic
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