05-1250
Anti-Trimethyl Histone H3(Lys9) Antibody, clone CMA308
clone CMA308, from mouse
Synonym(s):
H3K9me3, Histone H3 (tri methyl K9), H3 histone family, member T, histone 3, H3, histone cluster 3, H3
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
mouse
Quality Level
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
CMA308, monoclonal
species reactivity
vertebrates, human
technique(s)
ELISA: suitable
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
multiplexing: suitable
western blot: suitable
isotype
IgG1κ
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
trimethylation (Lys9)
Gene Information
human ... H3C1(8350)
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. Histone proteins are highly post-translationally modified however Histone H3 is the most extensively modified of the five histones. Histone H3 sequence variants and variable modification states are thought to play a role in the dynamic and long term regulation of genes. Trimethylation of histone H3 on Lys9 (H3K9me3) is one of the most highly studied epigenetic marks. H3K9me3 functions in the repression of euchromatic genes, and in epigenetic control of heterochromatin assembly, most likely by acting as a recognition motif for the binding of chromatin-associated proteins, such as Swi6 or HP1α. The enzymes responsible for H3K9 trimethylation are SUV39H1 and SUV39H2.
Specificity
Broad species cross-reactivity is expected, based on sequence homology.
This antibody recognizes Histone H3 trimethylated at Lys9. Some cross-reactivity with dimethyl Lys9 is detected at higher concentrations, but the difference in specificity is >27-fold1. Phosphorylation of Ser10 interferes with antibody binding to trimethyl Lys91.
Immunogen
Epitope: Trimethyl Lys9
Synthetic peptide corresponding to amino acids 1-19 of human Histone H3, trimethylated on Lys9, conjugated to KLH.
Application
Anti-Trimethyl Histone H3(Lys9) Antibody, clone CMA308 is a mouse monoclonal antibody for detection of Trimethyl Histone H3(Lys9) also known as H3K9me3, Histone H3 (tri methyl K9) & has been validated in WB, ELISA, ICC, IP, Mplex.
ELISA:
This antibody has been shown by an outside laboratory to be suitable for ELISA.1
Immunoprecipitation:
This antibody has been shown by an outside laboratory to be suitable for IP.1
Immunocytochemistry:
This antibody has been shown by an outside laboratory to be suitable for immunocytochemistry.1
This antibody has been shown by an outside laboratory to be suitable for ELISA.1
Immunoprecipitation:
This antibody has been shown by an outside laboratory to be suitable for IP.1
Immunocytochemistry:
This antibody has been shown by an outside laboratory to be suitable for immunocytochemistry.1
Research Category
Epigenetics & Nuclear Function
Epigenetics & Nuclear Function
Research Sub Category
Histones
Histones
Quality
Western Blot Analysis:
A 0.5 – 2 μg/mL dilution of this antibody detected histone H3 in 10 μg of HeLa acid extract.
A 0.5 – 2 μg/mL dilution of this antibody detected histone H3 in 10 μg of HeLa acid extract.
Target description
~17 kDa
Physical form
Format: Purified
Protein G Purified
Purified mouse monoclonal IgG1κ in PBS with 0.05% sodium azide.
Storage and Stability
Stable for 1 year at 2-8°C from date of receipt. For maximum recovery of product, centrifuge the vial prior to removing the cap. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Analysis Note
Control
HeLa Acid extract.
HeLa Acid extract.
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.
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wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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’.
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Find documentation for the products that you have recently purchased in the Document Library.
E Gonzalez-Munoz et al.
Scientific reports, 9(1), 8632-8632 (2019-06-16)
Mouse and cell-based studies have shown that macroH2A histone variants predominantly associate with heterochromatin. Functional studies found that macroH2As are involved in gene repression, inhibiting the acquisition of pluripotency and preserving cell differentiation. However, only a few studies have analysed
The organization of histone H3 modifications as revealed by a panel of specific monoclonal antibodies.
Kimura, Hiroshi, et al.
Cell Structure and Function, 33, 61-73 (2008)
J K Wiencke et al.
Oncogene, 27(17), 2412-2421 (2007-10-31)
Histone H3 lysine 9 trimethylation (H3K9Me3) has been associated with transcriptional repression, but recent findings implicate this chromatin modification in transcriptional activation and mRNA elongation by RNA polymerase II. Here, we applied immunoprecipitation (IP) with a custom DNA tiling microarray
Xuncheng Liu et al.
Plant physiology, 158(1), 119-129 (2011-10-14)
The molecular mechanism of how the histone deacetylase HDA6 participates in maintaining transposable element (TE) silencing in Arabidopsis (Arabidopsis thaliana) is not yet defined. In this study, we show that a subset of TEs was transcriptionally reactivated and that TE
Kristina Ivanauskiene et al.
Genome research, 24(10), 1584-1594 (2014-07-23)
Histone variant H3.3 is deposited in chromatin at active sites, telomeres, and pericentric heterochromatin by distinct chaperones, but the mechanisms of regulation and coordination of chaperone-mediated H3.3 loading remain largely unknown. We show here that the chromatin-associated oncoprotein DEK regulates
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