MABE1119
Anti-H2AK15ub Antibody, clone EDL H2AK15-4
clone EDL H2AK15-4, from mouse
Synonym(s):
Histone H2A, H2A, Histone H2A1
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.43
Recommended Products
biological source
mouse
Quality Level
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
EDL H2AK15-4, monoclonal
species reactivity
Drosophila, human, mouse
technique(s)
immunocytochemistry: suitable
western blot: suitable
isotype
IgG2bκ
NCBI accession no.
UniProt accession no.
shipped in
ambient
target post-translational modification
unmodified
Gene Information
human ... HIST1H2AG(8969)
General description
Histone H2A is one of four components of the core nucleosomal structure. 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. The degree of ubiquitylation at DNA damage sites is regulated at multiple levels in order to generate proper DNA damage response. Uncontrolled ubiquitylation of histones can lead to unscheduled transcriptional silencing and generate defects in DNA damage checkpoint activation and cell cycle arrest. The RNF168 E3 ligase ubiquitylates H2A at K13, K15, which in turn triggers the recruitment of DNA damage response proteins, such as 53BP1 and BRCA1 to DNA break sites. USP51, a deubiquitinating enzyme, removes H2AK13, 15ub following DNA repair. Depletion of USP51 can result in elevated levels of H2AK13, 15ub on chromatin and cause delays in disassembly of proteins at DNA damage foci.
Specificity
Clone EDL H2AK15-4 specifically recognizes histone H2A monoubiquitylated at Lys15, but not unmodified H2A. Does not recognize di-ubiquitin, K63 and K27 linked di-ubiquitin species.
Immunogen
KLH-conjugated branched peptide corresponding to the ubiquitination site on human H2AK15.
Application
Anti-H2AK15ub, clone EDL H2AK15-4, Cat. No. MABE1119, is a highly specific mouse monoclonal antibody, that targets H2A ubiquitylated at Lys15 and has been tested in Immunocytochemistry and Western Blotting.
Western Blotting Analysis: A representative lot detected H2AK15ub in U2OS cells with or without RNF168 depletion (Wang, Z., et. al. (2016). Genes Dev. 30(8):946-59).
Immunocytochemistry Analysis: A representative lot detected H2AK15ub in U2OS cells (Wang, Z., et. al. (2016). Genes Dev. 30(8):946-59).
Immunocytochemistry Analysis: A representative lot detected H2AK15ub in U2OS cells (Wang, Z., et. al. (2016). Genes Dev. 30(8):946-59).
Quality
Evaluated by Western Blotting in Ub-Lysine15 H2A and H2AK13, 15R nucleosome lysates.
Western Blotting Analysis: 2 ug/mL of this antibody detected Ub-Lysine15 H2A and H2AK13, 15R nucleosome lysates.
2 mg/mL
Western Blotting Analysis: 2 ug/mL of this antibody detected Ub-Lysine15 H2A and H2AK13, 15R nucleosome lysates.
2 mg/mL
Target description
~25 kDa observed. Uncharacterized bands may be observed in some lysate(s).
Physical form
Format: Purified
Other Notes
Concentration: Please refer to lot specific datasheet.
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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Certificates of Analysis (COA)
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Vincent Gaggioli et al.
Nature cell biology, 25(7), 1017-1032 (2023-07-07)
Chromatin is dynamically reorganized when DNA replication forks are challenged. However, the process of epigenetic reorganization and its implication for fork stability is poorly understood. Here we discover a checkpoint-regulated cascade of chromatin signalling that activates the histone methyltransferase EHMT2/G9a
Lei Zhang et al.
Nature communications, 13(1), 360-360 (2022-01-20)
Human 53BP1 is primarily known as a key player in regulating DNA double strand break (DSB) repair choice; however, its involvement in other biological process is less well understood. Here, we report a previously uncharacterized function of 53BP1 at heterochromatin
Mengfan Tang et al.
Cell reports, 32(6), 108018-108018 (2020-08-14)
53BP1 plays a central role in dictating DNA repair choice between non-homologous end joining (NHEJ) and homologous recombination (HR), which is important for the sensitivity to poly(ADP-ribose) polymerase inhibitors (PARPis) of BRCA1-deficient cancers. In this study, we show that FOXK1
Xia Ting et al.
Nucleic acids research, 47(18), 9721-9740 (2019-09-11)
How chromatin dynamics is regulated to ensure efficient DNA repair remains to be understood. Here, we report that the ubiquitin-specific protease USP11 acts as a histone deubiquitinase to catalyze H2AK119 and H2BK120 deubiquitination. We showed that USP11 is physically associated
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