

| Catalog No. | HP382014 | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Species reactivity | Human, Mouse | ||||||||
| Applications | ELISA, IHC, WB | ||||||||
| Host species | Rabbit | ||||||||
| Isotype | IgG | ||||||||
| 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. |
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| Product Usage Information |
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| 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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