Product Information

Contents: HDAC1 (C19) Blocking Peptide
Catalog Number: 66-P761
Sizes: 50 ug
Formulation: Each vial contains 100 μg of peptide in 0.5 ml PBS with 0.1% NaN₃ and 100 μg BSA.
Storage Conditions: Store at 4°C.
DO NOT FREEZE.

Available Formats of This Product
Cat. No.	Format	Excite (nm)	Emit (nm)	Reported Applications
66-P761	Blocking Peptides for anti-mouse/human/rat HDAC1 polyclonal	N/A	N/A	WB

Questions? Please consult our answers to frequently asked questions at http://www.ebioscience.com/faq.

Description

This is 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. This blocking peptide has been reported for use in competition studies.

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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