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Merck

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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UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
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Nombre del producto

Anti-acetyl-Histone H3 (Lys14) Antibody, clone 13HH3-1A5, ascites fluid, clone 13HH3-1A5, from mouse

biological source

mouse

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)

Quality Level

Gene Information

human ... H3C1(8350)
mouse ... H3C1(360198)

Analysis Note

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.

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.

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.
~17 kDa observed. Uncharacterized bands may be observed at ~23 kDa and ~35 kDa in some cell lysates.

Immunogen

Ovalbumin-conjugated linear peptide corresponding to human Histone H3 acetylated at Lys14.

Physical form

Mouse monoclonal IgG1 in ascites containing 0.05% sodium azide.

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Clase de almacenamiento

12 - Non Combustible Liquids

wgk

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
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
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
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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SKUGTIN
MABE35104053252697760

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