MABE351
Anti-acetyl-Histone H3 (Lys14) Antibody, clone 13HH3-1A5
ascites fluid, clone 13HH3-1A5, from mouse
Sinónimos:
Histone H3.1t, H3/t, H3t, H3/g
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
biological source
mouse
Quality Level
antibody form
ascites fluid
antibody product type
primary antibodies
clone
13HH3-1A5, monoclonal
species reactivity
human, mouse
technique(s)
ChIP: suitable (ChIP-seq)
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG1
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
acetylation (Lys14)
Gene Information
human ... H3C1(8350)
mouse ... H3C1(360198)
General description
Histones are nuclear proteins that form octameric structures which bind DNA to form units of chromatin called nucleosomes. The family of histones—H2A, H2B, H3, and H4—are key players in gene regulation. They undergo a number of post-translational modifications (PTM) in response to various stimuli. Acetylation is a reversible PTM that involves the transfer of acetyl groups to N-terminal lysine (K) residues by a family of histone acetyltransferase enzymes, including GNAT, Gcn5, and p300/CBP. Histone acetylation reduces the electrostatic attractions between DNA and histones, which destabilizes chromatin structure and provide chromatin remodeling and transcriptional complexes, with access to DNA, potentially resulting in increased gene transcription. In fission yeast, acetylation of H3K4 is regulated by Gcn5 and the Mst2 complex, and is crucial to the activation of DNA damage checkpoint.
Immunogen
Ovalbumin-conjugated linear peptide corresponding to human Histone H3 acetylated at Lys14.
Application
Anti-acetyl-Histone H3 (Lys14) Antibody, clone 13HH3-1A5 is a mouse monoclonal antibody for detection of acetyl-Histone H3 (Lys14) also known as Histone H3.1t, H3/t, H3t, H3/g & has been validated in WB, IP, ICC.
Demonstrated to react in Mouse ESCs in ChIP-seq in Karmodiya et al. BMC Genomics 2012, 13:424.
Immunoprecipitation Analysis: A representative lot was used to immunoprecipitate acetyl-Histone H3 (Lys4) in IP.
Immunocytochemistry Analysis: A representative lot was used to detect acetyl-Histone H3 (Lys4) in ICC.
Chromatin Immunoprecipitation Analysis: A representative lot was used to detect acetyl-Histone H3 (Lys4) in ChIP.
Western Blot Analysis: A representative lot was used to detect acetyl-Histone H3 (Lys4) in WB.
Immunocytochemistry Analysis: A representative lot was used to detect acetyl-Histone H3 (Lys4) in ICC.
Chromatin Immunoprecipitation Analysis: A representative lot was used to detect acetyl-Histone H3 (Lys4) in ChIP.
Western Blot Analysis: A representative lot was used to detect acetyl-Histone H3 (Lys4) in WB.
Quality
Evaluated by Western Blot in HeLa acid extract.
Western Blot Analysis: A 1:2,000 dilution of this antibody detected acetyl-Histone H3 (Lys4) in 10 µg of HeLa acid extract.
Western Blot Analysis: A 1:2,000 dilution of this antibody detected acetyl-Histone H3 (Lys4) in 10 µg of HeLa acid extract.
Target description
~17 kDa observed. Uncharacterized bands may be observed at ~23 kDa and ~35 kDa in some cell lysates.
Physical form
Mouse monoclonal IgG1 in ascites containing 0.05% sodium azide.
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Storage Class
12 - Non Combustible Liquids
wgk_germany
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Renata Z Jurkowska et al.
Nature communications, 8(1), 2057-2057 (2017-12-14)
SETDB1 is an essential H3K9 methyltransferase involved in silencing of retroviruses and gene regulation. We show here that its triple Tudor domain (3TD) specifically binds to doubly modified histone H3 containing K14 acetylation and K9 methylation. Crystal structures of 3TD
Na Li et al.
Molecular cell, 63(3), 470-484 (2016-08-02)
Histone acetylation, including acetylated H3K14 (H3K14ac), is generally linked to gene activation. Monomethylated histone H3 lysine 4 (H3K4me1), together with other gene-activating marks, denotes active genes. In contrast to usual gene-activating functions of H3K14ac and H3K4me1, we here show that
Zhendong Cao et al.
Molecular cell, 81(17), 3604-3622 (2021-08-07)
The transformed state in acute leukemia requires gene regulatory programs involving transcription factors and chromatin modulators. Here, we uncover an IRF8-MEF2D transcriptional circuit as an acute myeloid leukemia (AML)-biased dependency. We discover and characterize the mechanism by which the chromatin
Kyong-Rim Kieffer-Kwon et al.
Molecular cell, 67(4), 566-578 (2017-08-15)
50 years ago, Vincent Allfrey and colleagues discovered that lymphocyte activation triggers massive acetylation of chromatin. However, the molecular mechanisms driving epigenetic accessibility are still unknown. We here show that stimulated lymphocytes decondense chromatin by three differentially regulated steps. First
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