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SAB4300213

Sigma-Aldrich

Anti-phospho-H2AFX (pSer139) antibody produced in rabbit

affinity isolated antibody

Synonym(s):

Anti-H2A histone family, member X antibody produced in rabbit, Anti-H2A.X antibody produced in rabbit, Anti-H2A/X antibody produced in rabbit, Anti-H2AX antibody produced in rabbit

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About This Item

MDL number:
MFCD07370338
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

~15 kDa

species reactivity

human

concentration

1 mg/mL

technique(s)

indirect immunofluorescence: 1:100-1:200
western blot: 1:500-1:1000

isotype

IgG

immunogen sequence

(Q-A-SP-Q-E)

NCBI accession no.

NP_002096.1

UniProt accession no.

P16104

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

phosphorylation (pSer139)

Gene Information

human ... H2AFX(3014)

Related Categories

Immunogen

Peptide sequence around phosphorylation site of serine 139 (Q-A-S(p)-Q-E), according to the protein H2AFX.

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Target description

Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation.

Physical form

Solution in phosphate-buffered saline containing 0.02% sodium azide and 50% glycerol

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

10 - 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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Eva Pagáčová et al.
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Diverse stresses including genotoxic therapy can induce proliferating cancer cells to undergo cellular senescence and take on the characteristic phenotypes of replicative cellular aging. This accelerated or therapy-induced senescence has been alternatively proposed to contribute to therapeutic efficacy or resistance.
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Senescence is a tumor-suppressive mechanism induced by telomere shortening, oncogenes, or chemotherapy treatment. Although it is clear that this suppressive pathway leads to a permanent arrest in primary cells, this might not be the case in cancer cells that have
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As a transcriptional repressor, Chromobox 8 (CBX8) overexpression is found to be associated with tumorigenesis in several cancers. However, its role in radiotherapy resistance remains poorly characterized. Our study is the first to explore the correlation between CBX8 and radioresistance.
Jingjing Luo et al.
Clinical cancer research : an official journal of the American Association for Cancer Research, 25(2), 808-818 (2018-09-07)
We previously reported preventive and therapeutic effects of Smad7, a multifunctional protein, on radiotherapy (RT)-induced mucositis in mice without promoting human oral cancer cell survival or migration in vitro. The current study aims to determine whether a Smad7-based biologic can
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