Skip to Content
MilliporeSigma
All Photos(2)

Key Documents

SAB4200609

Sigma-Aldrich

Monoclonal Anti-diMethyl-Histone H3 (diMe-Lys9) (H3K9me2) antibody produced in mouse

~1.0 mg/mL, clone 5E5-G5, purified immunoglobulin

Synonym(s):

Anti-H3F3A H3.3A H3F3 PP781 H3F3B H3.3B, Anti-HIST1H3A H3FA, Anti-HIST1H3B H3FL, Anti-HIST1H3C H3FC, Anti-HIST1H3D H3FB, Anti-HIST1H3E H3FD, Anti-HIST1H3F H3FI, Anti-HIST1H3G H3FH, Anti-HIST1H3H H3FK, Anti-HIST1H3I H3FF, Anti-HIST1H3J H3FJ, Anti-HIST2H3A HIST2H3C H3F2 H3FM HIST2H3D

Sign Into View Organizational & Contract Pricing


About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

5E5-G5, monoclonal

form

buffered aqueous solution

mol wt

antigen ~17 kDa

concentration

~1.0 mg/mL

technique(s)

immunoblotting: 2-4 μg/mL using histones isolated from human HeLa cells.
immunofluorescence: 1-2 μg/mL using human HeLa cells.

isotype

IgG1

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

dimethylation (Lys9)

General description

Monoclonal Anti-diMethyl-Histone H3 (diMe-Lys9) (H3K9me2) (mouse IgG1 isotype) is derived from the hybridoma 5E5-G5 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a dimethylated (diMe-Lys9) peptide corresponding to the N-terminus of human histone H3, conjugated to KLH. Histones H3 and H4 are the core histones forming nucleosome, which is the fundamental unit of chromatin. H3 and H4 remodified by methylation and are highly methylated in mammalian cells.

Immunogen

dimethylated (diMe-Lys9) peptide corresponding to the N-terminus of human histone H3, conjugated to KLH. The isotype is determined by ELISA using Mouse Monoclonal Antibody Isotyping Reagents (Sigma ISO-2).

Application

Monoclonal Anti-diMethyl-Histone H3 (diMe-Lys9) (H3K9me2) antibody produced in mouse may be used in several immunochemical techniques including immunoblotting (~17 kDa) and immunofluorescence.

Biochem/physiol Actions

Histones are subjected to extensive covalent modifications, including phosphorylation, methylation, acetylation and ubiquitination thought to play an important role in development and in cancer. Histone methylation, is a complex, dynamic process involving various biological processes including transcriptional regulation, chromatin condensation, mitosis and heterochromatin assembly. Moreover, lysine residues can be mono-, di-, and tri-methylated, adding further complexity to the regulation of chromatin structure. Conserved lysine residues in the N-terminal tail domains of histone H3, Lys4, Lys9 and Lys27 are the preferred sites of methylation. Methylation of H3 at Lys9 is a modification intrinsically linked to epigenetic silencing and heterochromatin assembly.

Physical form

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

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

10 - Combustible liquids

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’.

Already Own This Product?

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

Visit the Document Library

Cancer epigenetics: from mechanism to therapy
Dawson M A and Kouzarides T
Cell, 150(1), 12-27 (2012)
Histone methylation versus histone acetylation: new insights into epigenetic regulation
Rice JC, et al.
Current Opinion in Cell Biology, 13(3), 263-273 (2001)
Chromatin modifications and their function
Kouzarides, Tony
Cell, 128(4), 693-705 (2007)

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