HDAC9 (N-terminus)Rabbit anti-Human, Polyclonal, Rockland™

Description

• Store vial at -20°C prior to opening
• Aliquot contents and freeze at -20°C or below for extended storage
• Avoid cycles of freezing and thawing
• Centrifuge product if not completely clear after standing at room temperature
• This product is stable for several weeks at 4°C as an undiluted liquid
• Dilute only prior to immediate use
• A BLAST analysis was used to suggest cross-reactivity with human based on 100% sequence homology
• Cross-reactivity with HDAC9 from other sources has not been determined
• In the intact cell, DNA closely associates with histones and other nuclear proteins to form chromatin
• The remodeling of chromatin is a critical component of transcriptional regulation and the acetylation of nucleosomal histones is a major source of this remodeling
• Acetylation of lysine residues in the amino terminal tail domain of histone results in an allosteric change in the nucleosomal conformation and an increased accessibility to transcription factors by DNA
• Several mammalian proteins function as nuclear histone acetylases, including GCN5, PCAF (p300/CBP-associated factor), p300/CBP, HAT1 and the TFIID subunit TAF II p250
• Conversely, the deacetylation of histones is associated with transcriptional silencing
• The histone deacetylases (HDAC) include HDAC1-9
• HDAC9 and HDAC9a are two alternatively spliced isoforms of HDAC9
• HDAC9a is 132 amino acids shorter than HDAC9, but both isoforms contain the HDAC catalytic domain, remain capable of deacetylase activity and repress myoctye enhancer-binding factor 2-mediated transcription
• HDAC9 and HDAC9a are expressed in brain, skeletal muscle, kidney, placenta and pancreas.