Anti-acetyl-Histone H3 (Lys9) Antibody

serum, Upstate®

H3K9Ac, Histone H3 (acetyl K9), H3 histone family, member T, histone 3, H3, histone cluster 3, H3

origen biológico


Nivel de calidad


forma del anticuerpo


antibody product type

primary antibodies



species reactivity

yeast, Saccharomyces cerevisiae, vertebrates, human




ChIP: suitable (ChIP-seq)
multiplexing: suitable
western blot: suitable



Nº de acceso NCBI

Nº de acceso UniProt

enviado en

dry ice

Descripción general

Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the ′beads on a string′ structure. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine.


Recognizes acetyl-histone H3 (Lys9), Mr 17 kDa. An additional unknown protein was detected at Mr 23 kDa.
Broad species-cross reactivity is expected.


Epitope: a.a. 4-14
Ovalbumin-conjugated, synthetic peptide (KQTARAcKSTGGK-C) corresponding to amino acids 4-14 of yeast histone H3 acetylated on lysine 9, with a C-terminal cysteine added for conjugation purposes.


Chromatin Immunoprecipitation (ChIP):
An independent laboratory has shown this antibody preferentially immunoprecipitates chromatin from wild type yeast and not from a yeast strain containing a Lysine substitution to Alanine at residue 9.

Beadlyte Histone-Peptide Specificity Assay:
A 1:1000-1:5000 dilution of this lot was incubated with histone H3 peptides containing various modifications conjugated to Luminex microspheres. No cross-reactivity with peptides containing acetyl-lysine 14 or acetyl-lysine 27 was observed.
Anti-acetyl-Histone H3 (Lys9) Antibody is a Rabbit Polyclonal Antibody for detection of acetyl-Histone H3 (Lys9) also known as H3K9Ac, Histone H3 (acetyl K9) and has been published and validated in ChIP, WB, Mplex.
Research Sub Category
Research Category
Epigenetics & Nuclear Function


Routinely evaluated by western blot on acid extracts from sodium butyrate treated HeLa cells.

Western Blot Analysis:
A 1:5000-1:10,000 dilution of this lot detected acetyl-Histone H3 (Lys9) in acid extracts from sodium butyrate treated HeLa cells (Catalog # 17-305).

Descripción de destino

17 kDa

Ligadura / enlace

Replaces: 04-1003

Forma física

Antiserum containing 0.35% sodium azide and 30% glycerol.

Almacenamiento y estabilidad

Stable for 1 year at -20°C from date of receipt. For maximum recovery of product, centrifuge the vial prior to removing the cap.

Nota de análisis

TSA-treated HeLa and NIH/3T3 cells, osteosarcoma tissue.

Otras notas

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Información legal

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Cláusula de descargo de responsabilidad

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.
Genome-wide profiling of histone H3 lysine 9 acetylation and dimethylation in Arabidopsis reveals correlation between multiple histone marks and gene expression.
Zhou J, Wang X, He K, Charron JB, Elling AA, Deng XW
Plant Molecular Biology null
Genome-wide analysis of abnormal H3K9 acetylation in cloned mice.
Suzuki, T; Kondo, S; Wakayama, T; Cizdziel, PE; Hayashizaki, Y
Testing null
CBP/p300-mediated acetylation of histone H3 on lysine 56.
Das, C; Lucia, MS; Hansen, KC; Tyler, JK
Nature null
The transcription factor snail mediates epithelial to mesenchymal transitions by repression of estrogen receptor-alpha.
Dhasarathy, A; Kajita, M; Wade, PA
Molecular Endocrinology null
Histone deacetylase inhibitors modify pancreatic cell fate determination and amplify endocrine progenitors.
Haumaitre, Cecile, et al.
Molecular and cellular biology, 28, 6373-6383 (2008)

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