Histone H3

The relatively unstructured and highly charged N-terminal tail domains of histones are central to the processes that modulate chromatin structure. A diverse and elaborate array of post-translational modifications including acetylation, phosphorylation, and methylation occur on the N-terminal tail domains of histones, particularly of H3 and H4.1,2 These modifications may alter chromatin structure and recruit downstream chromatin-associated proteins involved in transcription regulation. These in turn, may dictate dynamic transitions between transcriptionally active or silent chromatin states.\nHistones H3 and H4 are the predominant histones modified by methylation and are highly methylated in mammalian cells.3,4 Histone methylation like acetylation is a complex dynamic process involved in a number of processes including transcriptional regulation, chromatin condensation, mitosis, and heterochromatin assembly. Moreover, lysine residues can be mono-, di-, and trimethylated at different heterochromatic subdomains adding further complexity to the regulation of chromatin structure.\nConserved lysines residues in the N-terminal tail domains of histone H3 (Lys4, Lys9, and Lys27) are the preferred sites of methylation.1,4-6 Histone H3 mono-, di-, and trimethylation at Lys4 and Lys9 are carried out both in vitro and in vivo by SET domain-, site-specific histone methyltransferases (HMTases), including Suv39h1, Suv39h2, and G9a.7,8 Di- and trimethylation of histone H3 at Lys4 in coding regions correlates with transcriptional activity of many genes.9,10 Dimethylation of Histone H3 at Lys4 occurs at both active and inactive euchromatic regions but not in silent heterochromatic sites, whereas trimethylation at Lys4 is present exclusively at active genes. Mono- and dimethylation of H3 at Lys9 are intrinsically linked to epigenetic silencing and heterochromatin assembly. In contrast, trimethylated H3 at Lys9 is enriched at pericentric heterochromatin domain.\n\nPositive Control: epitheloid carcinoma HeLa cells, human acute T cell leukema Jurkat cells and mouse fibroblast NIH3T3\n\nApplications: \nSuitable for use in Western Blot. Other applications not tested.\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot Store at -20 degrees C. Aliquots are stable for at least 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

H5110-12R2

Size

50ul

Applications

WB

Hosts

Rabbit

Reactivities

Hum

Form

0.01M PBS, pH 7.4

P Type

Pab

Purity

Purified by immunoaffinity chromatography.

References

1. Strahl, B.D., and Allis, C.D., Nature, 403, 41-45 (2000).\n2. Cheung, P., et al., Cell, 103, 263-271 (2000).\n3. Strahl, B.D., et al., Proc. Natl. Acad. Sci. USA, 96, 14967-14972 (1999).\n4. Rice, J.C., and Allis,C. D., Curr. Opin. Cell Biol., 13, 263-273 (2001).\n5. Jenuwien, T., and Allis, C.D., Science, 293, 1074-1080 (2001).\n6. Bird, A., Science, 294, 2113-2115 (2001).\n7. Rea, S., et al., Nature, 406, 593-599 (2000).\n8. Rice, J.C., et al., Mol. Cell, 12, 1591-1598 (2003).\n9. Bernstein, B.E., et al., Proc. Natl. Acad. Sci. USA, 99, 8695-8700 (2002).\n10. Santos-Rosa, H., et al., Nature, 419, 407-411 (2002).\n11. Lachner, M., et al., Nature, 410, 116-120 (2001).\n12. Bannister, A.J., et al., Nature, 410, 120-124 (2001).\n13. Nakayama, J-I., et al., Science, 292, 110-113 (2001).\n14. Noma, K-I., et al., Science, 293, 1150-1155 (2001).

Additional Info

Detects a band at approximately 17kD. Partial or no inhibition is observed with the di-methylated histone H3 [diMe-Lys4 ] peptide (human, amino acids 1-8) and the non-methylated histone H3 peptide (human, amino acids 1-8). Species Crossreactivity: Crossreacts with Human.

Alternative Names

H3, HisH3, His1H3, H3/a, H3/b, H3/c, H3/d, H3/f, H3/h, H3/i, H3/j, H3/k, H3/l