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SAB4200609

Sigma-Aldrich

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

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

Synonyme(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

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

5E5-G5, monoclonal

Forme

buffered aqueous solution

Poids mol.

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

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

dimethylation (Lys9)

Description générale

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.

Immunogène

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.

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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

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