06-599

Sigma-Aldrich

Anti-acetyl-Histone H3 Antibody

from rabbit

Synonym(s):
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 antibody

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human, mouse, rat

application(s)

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

NCBI accession no.

UniProt accession no.

shipped in

wet ice

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. Acetylation of histone H3 occurs at several different lysine positions in the histone tail and is performed by a family of enzymes known as Histone Acetyl Transferases (HATs). Acetylation of lysine14 is commonly seen in genes that are being actively transcribed into RNA.

Specificity

Recognizes Histone H3 acetylated at the N-terminus.
Broad species cross-reactivity expected based on sequence similarity.

Immunogen

Epitope: N-terminus.
Linear peptide corresponding to human Histone H3 acetylated at the N-terminus.

Application

Detect acetyl-Histone H3 with Anti-acetyl-Histone H3 Antibody (Rabbit Polyclonal Antibody), that has been shown to work in WB, ICC, ChIP, ChIP-seq.
Research Sub Category
Histones
Research Category
Epigenetics & Nuclear Function
Immunocytochemistry Analysis: 1:500 dilution of a representative lot of this antibody detected acetylated Histone H3 in NIH/3T3 and A431 cells.

Chromatin Immunoprecipitation: This antibody has been shown to work for chIP using HeLa extracted chromatin and 5 mg of this antibody.

ChIP-Seq: This antibody has been shown to work for ChIP-Seq in Kanai, A., et. al. (2011). DNA Research 18:379-392.

Quality

Evaluated by Western Blot in HeLa acid extract, sodium butyrate treated HeLa cells, and recombinant Histone H3.

Western Blot Analysis: 0.05 µg/mL of this antibody detected Histone H3 on 10 µg of HeLa acid extract, sodium butyrate treated HeLa cells, and recombinant Histone H3.

Target description

~ 17 kDa observed

Physical form

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

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Analysis Note

Control
HeLa acid extract, sodium butyrate treated HeLa cells, and recombinant Histone H3

Other Notes

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

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_code

12 - Non Combustible Liquids

WGK Germany

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

Differences in stability of repressor complexes at promoters underlie distinct roles for Rb family members.
Young, AP; Longmore, GD
Oncogene null
Deletion of the major GATA1 enhancer HS 1 does not affect eosinophil GATA1 expression and eosinophil differentiation.
Guyot, B; Valverde-Garduno, V; Porcher, C; Vyas, P
Blood null
Promoter-specific p53-dependent histone acetylation following DNA damage.
Kaeser, MD; Iggo, RD
Oncogene null
Coregulator recruitment and histone modifications in transcriptional regulation by the androgen receptor.
Kang, Z; Janne, OA; Palvimo, JJ
Molecular Endocrinology null
CBP recruitment and histone acetylation in differential gene induction by glucocorticoids and progestins.
Lambert, JR; Nordeen, SK
Molecular Endocrinology null

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