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06-942

Sigma-Aldrich

Anti-acetyl-Histone H3 (Lys9) Antibody

Upstate®, from rabbit

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Synonym(s):
H3K9Ac, Histone H3 (acetyl K9), H3 histone family, member T, histone 3, H3, histone cluster 3, H3
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

polyclonal

species reactivity

mouse, human, rat

manufacturer/tradename

Upstate®

technique(s)

ChIP: suitable (ChIP-seq)
dot blot: suitable
flow cytometry: suitable
western blot: suitable

isotype

IgG

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

acetylation (Lys9)

Gene Information

human ... HIST1H3F(8968)

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This Item
ABE1807-35207-450
antibody form

purified immunoglobulin

antibody form

affinity isolated antibody

antibody form

serum

antibody form

purified immunoglobulin

species reactivity

mouse, human, rat

species reactivity

chicken, human, mouse

species reactivity

human, Saccharomyces cerevisiae, yeast, vertebrates

species reactivity

chicken, mouse, human

biological source

rabbit

biological source

rabbit

biological source

rabbit

biological source

rabbit

shipped in

dry ice

shipped in

wet ice

shipped in

dry ice

shipped in

wet ice

technique(s)

ChIP: suitable (ChIP-seq), flow cytometry: suitable, dot blot: suitable, western blot: suitable

technique(s)

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

technique(s)

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

technique(s)

dot blot: suitable, immunocytochemistry: suitable, inhibition assay: suitable (peptide), western blot: suitable

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General description

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.

Specificity

Histone H3 acetylated at position 9.
although this peptide sequence is identical in a wide range of animal and plant species.

Immunogen

Epitope: Surrounding H3K9ac
KLH-conjugated synthetic peptide (ARTKQTARK(Ac)STG-C) corresponding to amino acids 1-12 of Histone H3 with acetylated Lys9.

Application

Anti-acetyl-Histone H3 (Lys9) Antibody is a Rabbit Polyclonal Antibody for detection of Histone H3 acetylated on lysine 9. This purified Ab, also known as Anti-H3K9Ac, is specificity verified by dot blot (DB), published in peer reviewed journals, and validated in WB, ChIP, ChIP-seq, FC.
Chromatin Immunoprecipitation/ChIP-seq Analysis: A representative lot immunoprecipitated acetyl-Histone H3 (Lys9) in 5 µg of HeLa cell lysate.
Dot Blot Analysis: A 1:1,000 dilution from a representative lot detected acetyl-Histone H3 (Lys9) in an Absurance Histone H3 Antibody Specificity Array (Cat. No. 16-667) and an Absurance Histone H2A, H2B, H4 Antibody Specificity Array (Cat. No. 16-665).
Flow Cytometry Analysis: 0.25 µg of this antibody from a representative lot detected acetyl-Histone H3 (Lys9) in 1X10E6 HEK293 cells.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Histones

Quality

Evaluated by Western Blotting in sodium butyrate treated HeLa cell lysate.

Western Blotting Analysis: A 1:10,000 dilution of this antibody detected acetyl-Histone H3 (Lys9) in 10 µg of sodium butyrate treated HeLa cell lysate.

Target description

~17 kDa observed. Uncharacterized band(s) may appear in some lysates.

Linkage

Replaces: 04-1003

Physical form

Format: Purified
Protein A purified
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide with 30% glycerol.

Storage and Stability

Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Note: Variability in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.

Other Notes

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

Legal Information

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

Disclaimer

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.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1


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Myc and Miz-1 have coordinate genomic functions including targeting Hox genes in human embryonic stem cells.
Varlakhanova, N; Cotterman, R; Bradnam, K; Korf, I; Knoepfler, PS
Epigenetics & Chromatin null
Distinct patterns of histone methylation and acetylation in human interphase nuclei.
M Skalnikova, E Bartova, V Ulman, P Matula, D Svoboda, A Harnicarova, M Kozubek, S Kozubek
Physiological Research null
N-Myc regulates expression of pluripotency genes in neuroblastoma including lif, klf2, klf4, and lin28b.
Cotterman, R; Knoepfler, PS
Testing null
Chromatin decondensation and nuclear reorganization of the HoxB locus upon induction of transcription.
Chambeyron, S; Bickmore, WA
Genes & Development null
G9a/GLP histone lysine dimethyltransferase complex activity in the hippocampus and the entorhinal cortex is required for gene activation and silencing during memory consolidation.
Gupta-Agarwal, S; Franklin, AV; Deramus, T; Wheelock, M; Davis, RL; McMahon, LL; Lubin, FD
The Journal of Neuroscience null

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