2017 Histone H3K14 acetylation (H3k14ac) antibodies and relating products


1. Function of H3K14 acetylation (H3k14ac)

1.1 rDNA silencing and aging

Histone H3 N-terminal acetylation sites especially at K14 are important for rDNA silencing and aging, possibly through replication-dependent nucleosome assembly factor CAF-1. Both the H3K14 acetylation and deacetylation are specifically required to maintain RDN1 silencing. (1)

1.2 DNA repair

Histone H3 acetylation is induced by UV damage in yeast and may play an important role in the unfolding of strongly positioned nucleosomes during repair of UV damage. However, it remains elusive how H3 acetylation facilitates repair. Nucleosomes with H3K14ac have a higher affinity for purified chromatin remodeling complex RSC (Remodels the Structure of Chromatin) and show greater cyclobutane pyrimidine dimer repair compared with unacetylated nucleosomes. (2)


2. Interplay between H3k14 acetylation and other histone relating proteins.

2.1 Interplay with H3K9: Genome-wide H3K9ac and H3K14ac show very high correlation between each other as well as with other histone marks (such as H3K4me3) suggesting a coordinated regulation of active histone marks. Acetylation of H3K9 is mainly performed by histone acetyl transferases GCN5/PCAF and/or Tip60, whereas acetylation of H3K14 is mediated by GCN5/PCAF, p300/CBP and/or Myst3. (3)

2.2 GmPHD5: GmPHD5 interacts with other DNA binding proteins, including GmGNAT1 (an acetyl transferase), GmElongin A (a transcription elongation factor) and GmISWI (a chromatin remodeling protein). GmPHD5 can recognize specific histone methylated H3K4, with preference to di-methylated H3K4. The interaction between GmPHD5 and GmGNAT1 is regulated by the self-acetylation of GmGNAT1, which can also acetylate histone H3. GmGNAT1 exhibits a preference toward acetylated histone H3K14. There is a histone crosstalk between methylated H3K4 and acetylated H3K14. (4)

2.3 HBO1: The MYST histone acetyltransferase HBO1 (histone acetyltransferase bound to ORC; MYST2/KAT7) is essential for postgastrulation mammalian development. Lack of HBO1 led to a more than 90% reduction of histone 3 lysine 14 (H3K14) acetylation, whereas no reduction of acetylation was detected at other histone residues. (5)

2.4 Yng1: The PHD finger of Yng1, a subunit of the NuA3 histone acetyltransferase complex, recognizes methylated H3K4 and helps recruit this histone acetyltransferase complex for acetylation of H3K14. (6)

Check 2017 ChIP Validated Histone H4k20me antibodies. Epicypher validated Abcam OEM supplier:

More details about the supplier

Point 1
Validated Original manufacturer.

ABclonal Inc. is one of the original manufactures which is famous for its Epigenetics antibodies such as H3K4me antibody and H3K9me antibody. It is the long-term OEM supplier for many top10 antibody companies and we also visited their factory for double confirmation.

Point 2
Lot number management

Lot number is unique for each batch of antibody and it can be taken as identity number of antibody.  ABclonal has effective batch management and it helps you maximize the reproducibility. We will share everything about the antibodies basing on Lot number.

Point 3
Antibody validation for each batch.

ABclonal is performing strict antibody validation for each batch. WB, IHC, IF, DB and ChIP are performed to make sure each Histone antibody has strong specificity and no cross-reactivity for multiple applications. It is the only one of 52 Histone antibody suppliers which passed ChIP test by EpiCypher in 2017. (Paper to be published)

3. Relating protein study of H3K14ac

H3K14ac writer Find antibody Introduction Reference
GCN5 GCN5 antibody


Arabidopsis GCN5 found to be involved mostly in the acetylation of histone H3K9, K14 and K27, is shown to be required for the expression of a large number of genes, suggesting that this protein is involved in both long-term epigenetic regulation of chromatin modification and short-term control of transcriptional switches. Kim, W.H., Benhamed, M., Servet, C., Latrasse, D., Zhang, W., Delarue, M., and Zhou, D.X., (2009) Histone acetyltransferase GCN5 interferes with the miRNA pathway in Arabidopsis. Cell Research (2009) 19:899–909.
PCAF  PCAF antibody


Though p21 promoter occupancy by p53 was not altered by PCAF knockdown, activation of p21 transcription required an intact PCAF HAT domain, and induction of chromatin marks acetyl-H3K9 and acetyl-H3K14 at the p21 promoter by p53 was dependent upon physiologic levels of PCAF. Love I.M., Sekaric, P., Shi, D., Grossman, S.R., and Androphy, E.J., (2012) The histone acetyltransferase PCAF regulates p21 transcription through stress-induced acetylation of histone H3. Cell Cycle. 2012 Jul 1;11(13):2458-66.
CBP   CBP antibody


while p300 and CBP acetylate many common residues on H3 and H4, they do in fact possess very different specificities, and these specificities are dependent on whether histone or acetyl-CoA is limiting. Steady-state experiments with limiting H3 demonstrate that both CBP and p300 acetylate H3K14, H3K18, H3K23, with p300 having specificities up to 1010-fold higher than CBP. Ryan A.H., Kou, Y.M., and Andrews, A.J., (2013) Differences in Specificity and Selectivity Between CBP and p300 Acetylation of Histone H3 and H3/H4. Biochemistry. 2013 Aug 27; 52(34): 5746–5759.
p300  p300 antibody


p300 is a well known histone acetyltransferase and coactivator that plays pivotal roles in many physiological processes. Despite extensive research for the functions of p300 in embryogenesis and transcription regulation, its roles in regulating embryonic stem (ES) cell pluripotency are poorly understood. Zhong, X. and Jin, Y.,(2009) Critical Roles of Coactivator p300 in Mouse Embryonic Stem Cell Differentiation and Nanog Expression. The Journal of Biological Chemistry 284, 9168-9175.
Tip60  Tip60/KAT5 antibody


Tip60 expression is significantly correlated with cisplatin sensitivity in human lung cancer cell lines. Interestingly, the promoter region of the Tip60 gene contains several E boxes, and its expression was regulated by the E-box binding circadian transcription factor Clock but not by other E-box binding transcription factors such as c-Myc, Twist, and USF1. Hyperacetylation of H3K14 and H4K16 was found in cisplatin-resistant cells. Miyamoto, N. Izumi, H., Noguchi, T., Nakajima, Y., Ohmiya, Y., Shiota, M., Kidani, A., Tawara, A., and Kohno, K., (2008) Tip60 is regulated by circadian transcription factor clock and is involved in cisplatin resistance. J Biol Chem. 2008 Jun 27;283(26):18218-26.
Elp3   Elp3 was reported to preferentially acetylate H3K14 and H4K8, while Gcn5 has a more robust substrate population, including H3K9, H3K14, H3K18, and H3K23, but not H3K56. Turner, E.L., Malo, M.E., Pisclevich, M.G., Dash, M.D., Davies, G.F., Arnason, T.G., and Harkness, T.A.A., (2010) The Saccharomyces cerevisiae Anaphase-Promoting Complex Interacts with Multiple Histone-Modifying Enzymes To Regulate Cell Cycle Progression. Eukaryot Cell. 2010 Oct; 9(10): 1418–1431.
KAT12  KAT12 (GTF3C4) antibody


KATs, which are evolutionarily conserved from yeast to humans, catalyze the transfer of acetyl groups from acetyl-CoA onto lysine residues of acceptor proteins. Tapias, A., and Wang, Z.Q., (2017) Lysine Acetylation and Deacetylation in Brain Development and Neuropathies. Genomics Proteomics Bioinformatics. 2017 Feb; 15(1): 19–36.
TAF1   Acetylation of specific histone Lys residues, regulated by GCN5, TAF1, and HD1, is required for light-regulated gene expression. Benhamed, M., Bertrand, C., Servet, C., and Zhou, D.X., (2006) Arabidopsis GCN5, HD1, and TAF1/HAF2 interact to regulate histone acetylation required for light-responsive gene expression. Plant Cell. 2006 Nov;18(11):2893-903.
MOZ  MOZ (KAT8) antibody


Genome-wide mapping in erythroblasts demonstrated that BRD1 and HBO1 largely colocalize in the genome and target key developmental regulator genes. Of note, levels of global acetylation of histone H3 at lysine 14 (H3K14) were profoundly decreased in Brd1 deficient erythroblasts and depletion of Hbo1 similarly affected H3K14 acetylation. Mishima, Y., Miyagi, S., Saraya,A., Negishi, M., Endoh, M., Endo, T., Toytoda, T., Shinga, J., Katsumoto, T., Chiba, T., Yamaguchi, N., Kitabayashi, I., Koseki, H. and Iwama, A., (2011) The Hbo1-Brd1/Brpf2 complex is responsible for global acetylation of H3K14 and required for fetal liver erythropoiesis. Blood: 2011 118: 2443-2453
MORF   It has been have previously shown that the double plant homeodomain finger (DPF) of MORF is capable of binding to acetylated histone H3.The crystal structure of the MORF DPF-H3K14butyryl complex offers insight into the selectivity of this reader toward lipophilic acyllysine substrates. Klein, B.J., Simithy, J., Wang, X., Ahn, J., Andrews, F.H., Zhang, Y., Cote, J., Shi, X., Garcia, B.A., and Kutateladze, T.G., (2017) Recognition of Histone H3K14 Acylation by MORF. Structure. 2017 Apr 4;25(4):650-654.e2.
H3K14ac Readers Find antibody Introduction Reference
BRD4   BRD4, a protein known to be involved in acute myeloid leukemia and nuclear protein in testis midline carcinoma, recognizes the acetylation of histone H3 via its bromodomains. BRD4 preferentially acetylates histone H3 that is pre-acetylated at H3K14 lysine. Devaiah, B.N., Case-Borden, C., Gegonne, A., Hsu, C.H., Chen, Q.R., Meerzaman, D., Dey, A., Ozato, K., and Singer, D.S., (2016) BRD4 is a histone acetyltransferase that evicts nucleosomes from chromatin. Nature Structural & Molecular Biology 23, 540–548.
BAZ1B  BAZ1B antibody


The BAZ1B bromodomain displays affinity for several acetylated histone tail peptides, particularly ones incorporating H3K14(Ac). Gong. F., Chiu, L.Y., and Miller, K.M., (2016) Acetylation Reader Proteins: Linking Acetylation Signaling to Genome Maintenance and Cancer. PLoS Genet 12(9): e1006272. doi:10.1371/journal. pgen.1006272
BRG1   BRG1 (SMARCA4 ) antibody


The subunits, BAF45a and BAF45d, of Brg1 Associated Factors (BAF complex) specifically bind to acetylated lysine 14 of histone H3 (H3K14ac) via their PHD domains by peptide pulldown assays. This acetylation mark is found at enhancers by ChIPseq. Kim, A.Y.J. (2010) BAF complex association with enhancers and H3K14 acetylation in mouse embryonic stem cells. University of California, San Diego.



(1) Xu, H.H., Su, T., and Xue, Y., (2016) Histone H3 N-terminal acetylation sites especially K14 are important for rDNA silencing and aging. Scientific Reports 6, Article number: 21900.
(2) Duan M-R, Smerdon MJ. Histone H3 Lysine 14 (H3K14) Acetylation Facilitates DNA Repair in a Positioned Nucleosome by Stabilizing the Binding of the Chromatin Remodeler RSC (Remodels Structure of Chromatin). The Journal of Biological Chemistry. 2014;289(12):8353-8363. doi:10.1074/jbc.M113.540732.
(3) Karmodiya, K., Kred, A.R., Oulad-A.M., Kimura, H., and Tora, L., (2012) H3K9 and H3K14 acetylation co-occur at many gene regulatory elements, while H3K14ac marks a subset of inactive inducible promoters in mouse embryonic stem cells. BMC Genomics 13:424
(4) Wu, T., Pi, E.X., Tsai, S.N., Lam, H.M., Sun, S.M., Kwan, Y.W., and Ngai, S.M., (2011) GmPHD5 acts as an important regulator for crosstalk between histone H3K4 di-methylation and H3K14 acetylation in response to salinity stress in soybean. BMC Plant Biology 11:178
(5) Kueh, A., Dixon, M.P., Voss, A.K., and Thomas, T.,(2011) HBO1 Is Required for H3K14 Acetylation and Normal Transcriptional Activity during Embryonic Development. Mol. Cell. Biol. February 2011 vol. 31 no. 4 845-860
(6) Lee J-S, Smith E, Shilatifard A. The Language of Histone Crosstalk. Cell. 2010;142(5):682-685.