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Anti-Human EHMT2 Polyclonal Antibody (HP382014)

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Overview
Catalog No.HP382014
Species reactivityHuman, Mouse
ApplicationsELISA, IHC, WB
Host speciesRabbit
IsotypeIgG
Clonality Polyclonal
Immunogen E. coli - derived recombinant Human EHMT2 (Gly626-Thr918).
Target Histone H3-K9 methyltransferase 3, Histone-lysine N-methyltransferase EHMT2, BAT8, KMT1C, EHMT2, Euchromatic histone-lysine N-methyltransferase 2, H3-K9-HMTase 3, G9A, Lysine N-methyltransferase 1C, C6orf30, Protein G9a, HLA-B-associated transcript 8, NG36
Purification Purified by antigen affinity column.
Accession Q96KQ7
Form Liquid
Storage buffer 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Product Usage Information
Application Dilution
ELISA 1:5000-1:20000
IHC 1:50-1:500
WB 1:500-1:2000
Stability and Storage Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Background

Histone-lysine N-methyltransferase EHMT2 is a ~132 kDa protein. Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently.

1. Tachibana, M. et al. (2001) The Journal of biological chemistry 276, 25309-17. PMID: 11316813
2. Wu, H. et al. (2010) PloS one 5, e8570. PMID: 20084102
3. Yu, Y. et al. (2012) Molecular cell 46, 7-17. PMID: 22387026
4. Trojer, P. et al. (2009) The Journal of biological chemistry 284, 8395-405. PMID: 19144645
5. Huang, J. et al. (2010) The Journal of biological chemistry 285, 9636-9641. PMID: 20118233
6. Rathert, P. et al. (2008) Nature chemical biology 4, 344-6. PMID: 18438403
Note For research use only.
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