Skip to Content
Merck

MABE647

Sigma-Aldrich

Anti-acetyl-Histone H3 (Lys27) Antibody, clone RM172

clone RM172, from rabbit

Synonym(s):

Histone H3.3, Histone H3

Sign Into View Organizational & Contract Pricing

Select a Size

All Photos(2)

About This Item

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

biological source

rabbit

Quality Level

100

antibody form

purified antibody

antibody product type

primary antibodies

clone

RM172, monoclonal

species reactivity

human

technique(s)

multiplexing: suitable
western blot: suitable

isotype

IgG

UniProt accession no.

P84243

shipped in

wet ice

target post-translational modification

acetylation (Lys27)

Gene Information

human ... H3F3B(3021)

General description

Histone H3, also known as Histone H3.1t (H3/t), H3t, H3/g, and encoded by the gene name HIST3H3/ H3FT, is a core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Therefore, histones play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. 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. High levels of phosphorylation of Histone H3 are associated with mitosis.
~17 kDa observed. Uncharacterized bands may be observed in some lysate(s).

Immunogen

A linear peptide corresponding to human Histone H3 acetylated at Lys27.

Application

Multiplex Analysis (Mplex): 0.1-0.5 μg/mL from a representative lot was used in Multiplex.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Chromatin Biology
This Anti-acetyl-Histone H3 (Lys27) Antibody, clone RM172 is validated for use in Western Blotting, Multiplexing for the detection of acetyl-Histone H3.

Biochem/physiol Actions

This antibody reacts to Histone H3 acetylated at Lysine 27 (K27ac). No cross reactivity with other acetylated Lysines in Histone H3.

Physical form

Format: Purified
Protein A purified
Rabbit monoclonal in PBS with 1% BSA and 0.09% sodium azide

Preparation Note

Stable for 1 year at 2-8°C from date of receipt.
Note: Variability in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.

Analysis Note

Evaluated by Western Blotting in untreated and sodium butyrate treated HeLa acid extract.

Western Blotting Analysis (WB): 1 μg/mL of this antibody detected acetyl-Histone H3 (Lys27) in sodium butyrate treated HeLa acid extract.

Other Notes

Concentration: Please refer to lot specific datasheet.

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.

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

does not flash

Flash Point(C)

does not flash

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Michael S Hoetker et al.
Nature cell biology, 25(8), 1121-1134 (2023-07-18)
The epigenetic mechanisms that maintain differentiated cell states remain incompletely understood. Here we employed histone mutants to uncover a crucial role for H3K36 methylation in the maintenance of cell identities across diverse developmental contexts. Focusing on the experimental induction of
Marit W Vermunt et al.
Molecular cell, 83(5), 715-730 (2023-03-04)
Transcriptional enhancers have been extensively characterized, but cis-regulatory elements involved in acute gene repression have received less attention. Transcription factor GATA1 promotes erythroid differentiation by activating and repressing distinct gene sets. Here, we study the mechanism by which GATA1 silences
Chi Sun et al.
Scientific reports, 13(1), 12899-12899 (2023-08-10)
Enhancers function with a basal promoter to control the transcription of target genes. Enhancer regulatory activity is often studied using reporter-based transgene assays. However, unmatched results have been reported when selected enhancers are silenced in situ. In this study, using
Silvia Pomella et al.
Nature communications, 14(1), 8373-8373 (2023-12-16)
Rhabdomyosarcomas (RMS) are pediatric mesenchymal-derived malignancies encompassing PAX3/7-FOXO1 Fusion Positive (FP)-RMS, and Fusion Negative (FN)-RMS with frequent RAS pathway mutations. RMS express the master myogenic transcription factor MYOD that, whilst essential for survival, cannot support differentiation. Here we discover SKP2
Steven J Wu et al.
Nature biotechnology, 39(7), 819-824 (2021-04-14)
Methods for quantifying gene expression1 and chromatin accessibility2 in single cells are well established, but single-cell analysis of chromatin regions with specific histone modifications has been technically challenging. In this study, we adapted the CUT&Tag method3 to scalable nanowell and
View All Related Papers

Related Content

White Paper: Further considerations of antibody validation and usage.
Characterization of Estrogen Receptor α Phosphorylation Sites in Breast Cancer Tissue Using the SNAP i.d® 2.0 System

A major focus of breast cancer research is to understand the mechanisms responsible for disease progression and drug resistance. Toward that end, it has been found that approximately two thirds of all human breast carcinomas overexpress the Estrogen Receptor α (ERα) protein and it remains the primary pharmacological target for endocrine therapy1,2. The normal cellular function of ERα is as a transcription factor that mediates a wide variety of physiological processes, many of which are dependent upon phosphorylation of the receptor at specific amino acid residues3,4. Indeed, ERα is known to be phosphorylated at a multitude of different sites, yet how these all correlate to disease remains unclear5. Here, we interrogated multiple sites of ERα for phosphorylation status by screening an extensive panel of different breast cancer patient samples and other non-breast cancer tissue microarray (TMA) slide samples to determine their relevance to disease.

Global Trade Item Number

SKUGTIN
MABE64704055977181487

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service