深圳欣博盛生物科技有限公司

HDAC2 antibody [HDAC2-62]

histone deacetylase 2 , HD2 , KDAC2 , RPD3 , YAF1

Bovine, Chicken, Dog, Human, Mouse, Rat

Mouse

ELISA, ICC/IF, IHC, IP, WB

Monoclonal Anti-Histone Deacetylase 2 (HDAC2) recognizes human, bovine, dog, rat, mouse, and chicken HDAC2 (approx. 55 kDa). The antibody epitope resides within amino acids 471-488 of human HDAC2.

IgG2b

synthetic peptide corresponding to the C-terminal region of human histone deacetylase 2 (amino acid residues 471-488 with N-terminal added cysteine) conjugated to maleimide-activated KLH. This sequence is highly conserved in mouse and chicken (2 and 1 amino acid substitution, respectively).

Monoclonal

HDAC2-62

Purified immunoglobulin

Unconjugated

Batch dependent (Please refer to the vial label for the specific concentration.)

Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.

4°C

Liquid

PBS, 15mM Sodium azide.

GeneTex

The basic repeating unit of chromatin is the nucleosome, which is composed of a protein octamer containing two each of the core histones H2A, H2B, H3, and H4, surrounded by approximately 146 base pairs of DNA. Reversible acetylation of highly conserved lysine residues in the N-terminal tail domains of core histones plays an important role in transcriptional regulation, cell cycle progression, and development events. Several histone acetyltransferases (HATs) catalyze this acetylation reaction (e.g. GCN5, PCAF, p300/CBP, TAFII250, P/CAF, SRC-1, BRCA-2). Acetylation of the core histones is generally considered to be associated with gene activation, probably through maintenance of the unfolded structure of transcribing nucleosomes. Histone acetylation is a dynamic process in which levels are determined by the net activities of HATs and the competing enzymes histone deacetylases (HDACs). Both activities are associated with the nuclear matrix. Eleven different mammalian HDACs have been described. HDACs 1-3 & 8 (Class I) are similar to yeast Rpd3 protein, while HDACs 4-7, 9 & 10 (Class II) are similar to yeast Hda1 protein. The activities of the histone deacetylases are often, but not always, associated with transcriptional repression and nucleosome condensation. HDAC1, HDAC2 and several others are the catalytic subunits of different multiprotein regulatory complexes. Other components of such complexes may include: corepressors such as mSin3, N-CoR, SMRT, associated proteins such as SAP18, SAP30, RbAp46, RbAp48, and c-Ski oncogenic protein (involved in DNA methylation). Nucleosome remodeling and deacetylation (NRD) complexes containing HDAC1, HDAC2, Mi-2 (CH3, CH4) dermatomyositis specific autoantigen, and MAT2 (metastasis-associated protein) (related to MAT1) have been described. It is therefore assumed that ATP-dependent nucleosome remodeling activity and histone deacetylation may be interconnected or interdependent. Recruitment of the multiprotein complexes to promoter sites occurs by many sequence specific DNA-binding proteins such as unliganded nuclear hormone receptors, DP1-E2F, YY1, and Rb family of transcription factors, transcriptional repressors, and tumor suppressors (e.g. BRCA1). Aberrant recruitment of HDACs by various oncoproteins may occur in certain neoplastic diseases. It has been found that inhibition ofHDAC2 activity by valporic acid induces proteosomal degradation of HDAC2.