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Key Documents

05-636-AF555

Sigma-Aldrich

Anti-phospho-H2A.X Antibody (Ser139), clone JBW301, Alexa Fluor 555 Conjugate

clone JBW301, from mouse, ALEXA FLUOR 555

Synonim(y):

H2AXS139P, Histone H2A.X (phospho S139)

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About This Item

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

pochodzenie biologiczne

mouse

Poziom jakości

białko sprzężone

ALEXA FLUOR 555

forma przeciwciała

purified antibody

rodzaj przeciwciała

primary antibodies

klon

JBW301, monoclonal

reaktywność gatunkowa

human

reaktywność gatunkowa (przewidywana na podstawie homologii)

vertebrates (based on 100% sequence homology)

metody

immunocytochemistry: suitable

izotyp

IgG1

numer dostępu NCBI

numer dostępu UniProt

Warunki transportu

wet ice

docelowa modyfikacja potranslacyjna

phosphorylation (pSer139)

informacje o genach

human ... H2AX(3014)

Opis ogólny

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).

Zastosowanie

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).
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Histones

Jakość

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.

Opis wartości docelowych

17 kDa observed

Postać fizyczna

Protein G Purified
Purified mouse monoclonal IgG1 in buffer containing PBS with 15 mg/mL BSA and 0.1% azide

Przechowywanie i stabilność

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

Inne uwagi

Concentration: Please refer to lot specific datasheet.

Informacje prawne

ALEXA FLUOR is a trademark of Life Technologies

Oświadczenie o zrzeczeniu się odpowiedzialności

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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Kod klasy składowania

12 - Non Combustible Liquids

Klasa zagrożenia wodnego (WGK)

WGK 2

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

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Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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

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