|Presentation||Liquid suspension. Supplied as magnetic bead slurry in phosphate buffered saline, pH 7.4, containing 0.01% Tween®-20 and 0.09% sodium azide|
|Particle Size||~3 µm|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||Stable for 1 year at 2-8°C from date of shipment. Do Not Freeze.|
|Storage Temperature||2 to 8 °C|
|Material Size||10 reactions|
Magna ChIP™ Protein A Magnetic Beads -Trial Size MSDS
|Reference overview||Pub Med ID|
|The tumor suppressor p53 and histone deacetylase 1 are antagonistic regulators of the cyclin-dependent kinase inhibitor p21/WAF1/CIP1 gene.|
Lagger, Gerda, et al.
Mol. Cell. Biol., 23: 2669-79 (2003) 2003
The cyclin-dependent kinase inhibitor p21/WAF1/CIP1 is an important regulator of cell cycle progression, senescence, and differentiation. Genotoxic stress leads to activation of the tumor suppressor p53 and subsequently to induction of p21 expression. Here we show that the tumor suppressor p53 cooperates with the transcription factor Sp1 in the activation of the p21 promoter, whereas histone deacetylase 1 (HDAC1) counteracts p53-induced transcription from the p21 gene. The p53 protein binds directly to the C terminus of Sp1, a domain which was previously shown to be required for the interaction with HDAC1. Induction of p53 in response to DNA-damaging agents resulted in the formation of p53-Sp1 complexes and simultaneous dissociation of HDAC1 from the C terminus of Sp1. Chromatin immunoprecipitation experiments demonstrated the association of HDAC1 with the p21 gene in proliferating cells. Genotoxic stress led to recruitment of p53, reduced binding of HDAC1, and hyperacetylation of core histones at the p21 promoter. Our findings show that the deacetylase HDAC1 acts as an antagonist of the tumor suppressor p53 in the regulation of the cyclin-dependent kinase inhibitor p21 and provide a basis for understanding the function of histone deacetylase inhibitors as antitumor drugs.
|Distinct roles for Sp1 and E2F sites in the growth/cell cycle regulation of the DHFR promoter.|
Jensen, D E, et al.
J. Cell. Biochem., 67: 24-31 (1997) 1997
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