HDAC4 Polyclonal Antibody

Cayman Chemical Item Number 13494

Histone Deacetylase 4

Description

Antigen: synthetic peptide corresponding to amino acids 194-209 of human HDAC4 · Host: rabbit · Application(s): WB, IP, and ChIP · Histone deacetylase (HDAC) and histone acetyltransferase (HAT) are enzymes that regulate transcription by selectively deacetylating or acetylating the ε-amino groups of lysines located near the amino termini of core histone proteins.¹ Eleven members of HDAC family have been identified in the past several years.^2,3 These HDAC family members are divided into two classes, I and II. HDAC4 is a member of the class II family which also includes HDACs 5, 6, and 7, the molecular weights of which are all about two-fold larger than those of the class I members.

1 Meinke, P.T., and Liberator, P. Histone deacetylase: A target for antiproliferative and antiprotozoal agents. Curr Med Chem 8(2) 211-235 (2001).

2 Nakayama, T., and Takami, Y. Participation of histones and histone-modifying enzymes in cell functions through alterations in chromatin structure. J Biochem 129 491-499 (2001).

3 Rioli, V., Gozzo, F.C., Heimann, A.S., et al. Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotension-converting enzyme. J Biol Chem 278(10) 8547-8555 (2003).

Synonyms

Histone Deacetylase 4

Formulation

100 μg of protein G-purified IgG in 200 μl PBS containing 0.05% BSA and 0.05% sodium azide

Stability

1 year

Storage

-20°C

Shipping

Wet ice in continental US; may vary elsewhere

Specificity

Human HDAC4	+
Mouse HDAC4	+

Background Reading

Meinke, P.T., and Liberator, P. Histone deacetylase: A target for antiproliferative and antiprotozoal agents. Curr Med Chem 8(2) 211-235 (2001).

Nakayama, T., and Takami, Y. Participation of histones and histone-modifying enzymes in cell functions through alterations in chromatin structure. J Biochem 129 491-499 (2001).

Rioli, V., Gozzo, F.C., Heimann, A.S., et al. Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotension-converting enzyme. J Biol Chem 278(10) 8547-8555 (2003).

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1 ea

$234.00

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