Background: Interacts with key regulators (CBP, p300 and PCAF) of transcription and represses transcription. Acts as a histone-binding protein that regulates transcription. Acts as a deubiquitinating enzyme. Autosomal dominant cerebellar ataxias are a group of neuro-degenerative disorders caused by unstable CAG repeat expansions encoding polyglutamine tracts. Proteins with long polyglutamine tracts have an increased tendency to aggregate, often forming ubiquitinated intranuclear inclusion bodies. Machado-Joseph disease (MJD)/spinocerebellar ataxia type 3 (SCA3) gene encodes ataxin-3, which contains a polyglutamine stretch. Ataxin-3 is incorporated into most of the nuclear inclusions (NIs) and disappears from its normal cytoplasmic localization under pathological conditions in most neurons. However, in the early onset of SCA3, the association of a pathological form of ataxin-3 with nuclear matrix alters ataxin-3 conformation to expose the polyglutamine domain. In normal brain tissue, wild-type ataxin-3 can also be localized within the ubiquitin-positive nuclear inclusion, the Marinesco body, under certain stressful conditions on neuronal cells such as aging and polyglutamine neurotoxicity. Cells stably expressing ataxin-3 upregulate the mRNA levels of inflammatory response proteins, suggesting that inflammatory processes are involved in the pathogenesis of spinocerebellar ataxia type 3. Ataxin-3 binds to the N-terminus of two human homologs of the yeast DNA repair protein RAD23, HHR23A and HHR23B, which are important for nucleotide excision repair.

Description: Rabbit polyclonal to Ataxin 3

Immunogen: KLH conjugated synthetic peptide derived from Ataxin 3

Specificity:  ·Reacts with Human, Mouse and Rat.

·Isotype: IgG

Application:  ·Western blotting: 1/100-500. Predicted Mol wt: 42 kDa;

·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;

·Immunocytochemistry/Immunofluorescence: 1/100;

·Immunoprecipitation: 1/50;

·ELISA: 1/500;

·Optimal working dilutions must be determined by the end user.