Edit |   |
Antigenic Specificity | HDAC2 (C19) |
Clone | polyclonal |
Host Species | Rabbit |
Reactive Species | mouse, rat, human |
Isotype | n/a |
Format | unconjugated |
Size | 0.2 mg |
Concentration | 0.200 mg/ml |
Applications | Western Blot (WB) |
Reviews / Ratings | If you have used this antibody, please help fellow researchers by submitting reviews to pAbmAbs and antYbuddY. |
Description | Specificity: Mouse, rat, and human HDAC2. 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 HDA |
Immunogen | Immunogen: Synthetic peptide mapping to the carboxy terminal domain of human HDAC2. |
Other Names | [histone deacetylase 2; Histone deacetylase 2 variant; histone deacetylase 2; YY1-associated factor 1; transcriptional regulator homolog RPD3; histone deacetylase 2; Histone deacetylase 2 variant], [HDAC2; HD2; RPD3; YAF1] |
Gene, Accession # | [HDAC2], Gene ID: 3066, NCBI: NP_001518.2, UniProt: Q59GB9 |
Catalog # | MBS440063 |
Price | $240 |
Order / More Info | HDAC2 (C19) Antibody from MYBIOSOURCE INC. |
Product Specific 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. |