HP1γ Antibody

2619:

Flow , Immunofluorescence , Immunoprecipitation , Western Blotting

HP1γ Antibody detects endogenous levels of total HP1gamma protein. The antibody does not cross-react HP1alpha or HP1beta proteins.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the amino terminus of human HP1gamma. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western blot analysis of lysates from HeLa, NIH/3T3, C6 and COS cells, using HP1gamma antibody.

Flow Cytometry

Flow cytometric analysis of untreated HeLa cells, using HP1 gamma antibody (blue) compared to a nonspecific negative control antibody (red).

IF-IC

Confocal immunofluorescent image of HeLa cells labeled with HP1gamma Antibody (green). Actin filaments have been labeled with Alexa Fluor® 555 phalloidin (red). Blue pseudocolor = DRAQ5™ (fluorescent DNA dye).

Heterochromatin protein 1 (HP1) is a family of heterochromatic adaptor molecules involved in both gene silencing and higher order chromatin structure (1). All three HP1 family members (α, β, and γ) are primarily associated with centromeric heterochromatin; however, HP1β and γ also localize to euchromatic sites in the genome (2,3). HP1 proteins are approximately 25 kDa in size and contain a conserved amino-terminal chromodomain, followed by a variable hinge region and a conserved carboxy-terminal chromoshadow domain. The chromodomain facilitates binding to histone H3 tri-methylated at Lys9, a histone "mark" closely associated with centromeric heterochromatin (4,5). The variable hinge region binds both RNA and DNA in a sequence-independent manner (6). The chromoshadow domain mediates the dimerization of HP1 proteins, in addition to binding multiple proteins implicated in gene silencing and heterochromatin formation, including the SUV39H histone methyltransferase, the DNMT1 and DNMT3a DNA methyltransferases, and the p150 subunit of chromatin-assembly factor-1 (CAF1) (7-9). In addition to contributing to heterochromatin formation and propagation, HP1 and SUV39H are also found complexed with retinoblastoma (Rb) and E2F6 proteins, both of which function to repress euchromatic gene transcription in quiescent cells (10,11). HP1 proteins are subject to multiple types of post-translational modifications, including phosphorylation, acetylation, methylation, ubiquitination, and sumoylation, suggesting multiple means of regulation (12-14).

1. Maison, C. and Almouzni, G. (2004) Nat. Rev. Mol. Cell Biol. 5, 296-304.
2. Minc, E. et al. (2000) Cytogenet. Cell Genet. 90, 279-284.
3. Nielsen, A.L. et al. (2001) Mol. Cell 7, 729-739.
4. Lachner, M. et al. (2001) Nature 410, 116-120.
5. Bannister, A.J. et al. (2001) Nature 410, 120-124.
6. Muchardt, C. et al. (2002) EMBO Rep. 3, 975-981.
7. Yamamoto, K. and Sonoda, M. (2003) Biochem. Biophys. Res. Commun. 301, 287-292.
8. Fuks, F. et al. (2003) Nucleic Acids Res. 31, 2305-2312.
9. Murzina, N. et al. (1999) Mol. Cell 4, 529-540.
10. Nielsen, S.J. et al. (2001) Nature 412, 561-565.
11. Ogawa, H. et al. (2002) Science 296, 1132-1136.
12. Minc, E. et al. (1999) Chromosoma 108, 220-234.
13. Zhao, T. et al. (2001) J. Biol. Chem. 276, 9512-9518.
14. Lomberk, G. et al. (2006) Nat. Cell Biol. 8, 407-415.

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For Research Use Only. Not For Use In Diagnostic Procedures.