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Merck
CN

SAB4200045

Sigma-Aldrich

Anti-Dimethyl-Histone H3 (diMe-Lys27) antibody, Rat monoclonal

clone K27 8H2, purified from hybridoma cell culture

Synonym(s):

Anti-H3K27me2, Monoclonal Anti-Dimethyl-Histone H3 (diMe-Lys27) antibody produced in rat

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

Key Documents

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biological source

rat

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

K27 8H2, monoclonal

form

buffered aqueous solution

mol wt

antigen ~15 kDa

species reactivity

hamster, human, bovine, Drosophila, rat, mouse

technique(s)

immunocytochemistry: suitable
western blot: 0.25-0.5 μg/mL using HeLa cell extracts

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

dimethylation (Lys27)

Gene Information

bovine ... H3C1(517139)
human ... H3C1(8350)
mouse ... H3C1(360198)
rat ... H3C1(679994)

General description

Monoclonal Anti-dimethyl-Histone H3 (diMe-Lys27) (rat IgG2a isotype) is derived from the hybridoma K27 8H2 produced by the fusion of mouse myeloma cells and splenocytes from rat immunized with a synthetic methylated peptide.

Application

Monoclonal Anti-Dimethyl-Histone H3 (diMe-Lys27) antibody produced in rat may be used in immunoblotting and immunocytochemistry.

Biochem/physiol Actions

Methylation of histone H3 on Lys27 is associated with polycomb-mediated gene silencing in several systems. Mammals exhibit enrichment of [Me-Lys27] histone H3 at heterochromatin and [diMe-Lys27] histone H3 in euchromatin. [Me-Lys27] histone H3, also marks the inactive X chromosome. The relatively unstructured and highly charged N-terminal tail domains of histones are central to the processes that modulate chromatin structures such as acetylation, phosphorylation, and methylation, which occur particularly on Histones H3 and H4. Lysine residues can be mono-, di-, and trimethylated at different heterochromatic subdomains, adding further complexity to the regulation of chromatin structure. Conserved lysine residues in the N-terminal tail domain of histone H3, Lys4, Lys9 and Lys27 are the favored methylation sites.
Monoclonal Anti- dimethyl-Histone H3 (diMe-Lys27) specifically recognizes histone H3 dimethylated on Lys27 in human, bovine, mouse, rat, hamster, and Drosophila.

Physical form

Solution in 0.01M phosphate buffered saline pH 7.4, containing 15 mM sodium azide.

Preparation Note

Store at –20 °C. For continuous use, the product may be stored at 2–8 °C for up to one month. For extended storage, freeze at –20 °C in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

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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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
108M4800
119K4821

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Ikuhiro Okamoto et al.
Science (New York, N.Y.), 303(5658), 644-649 (2003-12-13)
The initiation of X-chromosome inactivation is thought to be tightly correlated with early differentiation events during mouse development. Here, we show that although initially active, the paternal X chromosome undergoes imprinted inactivation from the cleavage stages, well before cellular differentiation.
B D Strahl et al.
Nature, 403(6765), 41-45 (2000-01-19)
Histone proteins and the nucleosomes they form with DNA are the fundamental building blocks of eukaryotic chromatin. A diverse array of post-translational modifications that often occur on tail domains of these proteins has been well documented. Although the function of
Signaling to chromatin through histone modifications.
P Cheung et al.
Cell, 103(2), 263-271 (2000-11-01)
Antoine H F M Peters et al.
Molecular cell, 12(6), 1577-1589 (2003-12-24)
Methylation of position-specific lysine residues in histone N termini is a central modification for regulating epigenetic transitions in chromatin. Each methylatable lysine residue can exist in a mono-, di-, or trimethylated state, thereby extending the indexing potential of this particular

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