HDAC3 (C18) Antibody-Delta Biolabs

Product Info
Background	Histone deacetylases (HDACs) catalyze the removal of the acetyl modification on lysine residues of proteins, that includes the core nucleosomal histones H2A, H2B, H3, and H4 (1). HDACs together with HATs regulate the level of acetylation of the histones (1,2). The level of acetylation of nucleosomal histones plays a key regulatory role in the transcription of many genes (1,3). The repression of gene transcription is associated with the hypoacetylation of histones, while hyperacetylated histones are associated with the activation of transcription (1). Three classes of HDACs have been described and class I and II HDACs are structurally related. Class I HDACs consist of HDAC1, 2, 3, and 8. Class II HDACs consist of HDAC4, 5, 6, 7, 9, and 10. Class III HDACs are structurally unrelated to the human class I and II HDACs, and consist of homologues of the yeast Sir2 proteins (1).
Origin	HDAC3 (C18) is provided as an affinity purified rabbit polyclonal antibody, raised against a peptide mapping to the carboxy terminal domain of human HDAC3.
Form	200 �g/ml rabbit polyclonal IgG in 1 ml PBS containing 0.1 % sodium azide and 0.2% gelatin.
Immunogen	Synthetic peptide mapping to the carboxy terminal domain of human HDAC3.
Competition Studies	A blocking peptide is also available, DB073P, for use in competition studies. Each vial contains 0.100 mg of peptide in 0.5 ml PBS with 0.1% sodium azide and 100 mg BSA.
Product Details	Each vial contains 200 �g/ml of affinity purified rabbit IgG, HDAC1 (C19) DB071, in 1 ml PBS containing 0.1 % sodium azide and 0.2% gelatin.
Specificity	HDAC3 (C18) is recommended to detect mouse, rat, and human HDAC3.
Use	Western blotting. Recommended western blotting starting dilution 1:200.
Storage	Store this product at 4� C, do not freeze. The product is stable for one year from the date of shipment.
References	1.Richon VM and O�Brien JP. 2002. Histone Deacetylase Inhibitors: A New Class of Potential Therapeutic Agents for Cancer Research. Clinical Cancer Research 8(3): 662-664. 2.Lopez-Rodas G, Brosch G, Georgieva EI, Sendra R, Franco L and Loidl P. 1993. Histone deacetylase. A key enzyme for the binding of regulatory proteins to chromatin. FEBS Lett. 317(3): 175-180. 3.Riester D, Wegener D, Hildman C and Schwienhorst A. 2004. Members of the histone deacetylase superfamily differ in substrate specificity towards small synthetic substrates. Biochem Biophys Res Commun. 324(3): 116-1123.