Psmc1, Rabbit, Polyclonal Antibody, Abnova, Rabbit Polyclonal Antibody Raised Against Recombinant Psmc1, Each

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The 26s proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20s core and a 19s regulator. The 20s core is composed of 4 rings of 28 nonidentical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19s regulator is composed of a base, which contains 6 atpase subunits and 2 non-atpase subunits, and a lid, which contains up to 10 non-atpase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an atp/ubiquitin-dependent process in a nonlysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class i mhc peptides. This gene encodes one of the atpase subunits, a member of the triple-a family of atpases which have a chaperone-like activity. This subunit and a 20s core alpha subunit interact specifically with the hepatitis b virus x protein, a protein critical to viral replication. This subunit also interacts with the adenovirus e1a protein and this interaction alters the activity of the proteasome. Finally, this subunit interacts with ataxin-7, suggesting a role for the proteasome in the development of spinocerebellar ataxia type 7, a progressive neurodegenerative disorder. [Provided by refseqsequence: ydsnsggereiqrtmlellnqldgfdsrgdvkvimatnrietldpalirpgridrkiefplpdektkkrifqihtsrmtladdvtlddlimakddlsgadikaicteaglmalrerrmkvtnedfkkskenvlykkqegtpe