Contents: Affinity Purified anti-mouse/human/rat HDAC1 polyclonal
Catalog Number: 14-6761
Formulation: 200 µg/ml rabbit polyclonal IgG in PBS containing 0.1 % sodium azide and 0.2% gelatin.
Storage Conditions: Store at 4°C.
DO NOT FREEZE.
Clone: Polyclonal
Isotype: Rabbit IgG
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Description
The polyclonal antibody reacts with mouse, rat, and human HDAC1; the antibody was raised against a peptide mapping to the carboxy terminal domain of human HDAC1. HDAC1, the mammalian homologue of the yeast transcriptional regulator Rpd3p, was first purified using a trapoxin affinity matrix (1). Trapoxin is a cyclotetrapeptide that inhibits histone deacetylation in vivo and also correlates with an increase in the acetylation levels of all four core histones (1&2). These data support a role for HDAC1 as a key histone deacetylase. The function of HDAC1 has been further refined as responsible for the deacetylation of lysine residues on the N-terminal region of the core histones H2A, H2B, H3 and H4 (3&4).
Applications Reported
For research use only, not for diagnostic or therapeutic use. Purified anti-mo/hu/rat HDAC1 poly has been reported for use in immunoblotting (WB).
Applications Tested
Purified anti-mo/hu/rat HDAC1 poly has been tested by immunoblotting (WB). (1:200 starting dilution). It is recommended that this antibody be titrated for optimal performance in the assay of interest.
References
1. Taunton J, Hassig CA, Schreiber SL. 1996. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272:408-411.
2. Hassig CA, Tong JK, Fleischer TC, Owa T, Grable PG, Ayer DE, Schreiber SL. 1998. A role for histone deacetylase activity in HDAC1-mediated transcriptional repression. PNAS 95(7):3519-3524.
3. Lopez-Rodas G, Brosch G, Georgieva EI, Sendra R, Franco L, Loidl P. 1993. Histone deacetylase. A key enzyme for the binding of regulatory proteins to chromatin. FEBS lett 317(3):175-180.
4. Johnson CA, White DA, Lavender JS, O?Neill LP, Turner BM. 2002. Human class I histone deacetylase complexes show enhanced catalytic activity in the presence of ATP and co-immunoprecipitated with ATP-dependent charperone protein Hsp-70.
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