|Other Names||Proteasome subunit alpha type-1, 30 kDa prosomal protein, PROS-30, Macropain subunit C2, Multicatalytic endopeptidase complex subunit C2, Proteasome component C2, Proteasome nu chain, PSMA1, HC2, NU, PROS30, PSC2|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||HC2, NU, PROS30, PSC2|
|Function||The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Mediates the lipopolysaccharide-induced signal transduction in the macrophage proteasome (By similarity). Might be involved in the anti-inflammatory response of macrophages during the interaction with C.albicans heat-inactivated cells (By similarity).|
|Cellular Location||Cytoplasm. Nucleus.|
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Provided below are standard protocols that you may find useful for product applications.
The proteasome is a multicatalytic proteinase complex witha highly ordered ring-shaped 20S core structure. The core structureis composed of 4 rings of 28 non-identical subunits; 2 rings arecomposed of 7 alpha subunits and 2 rings are composed of 7 betasubunits. Proteasomes are distributed throughout eukaryotic cellsat a high concentration and cleave peptides in anATP/ubiquitin-dependent process in a non-lysosomal pathway. Anessential function of a modified proteasome, the immunoproteasome,is the processing of class I MHC peptides. This gene encodes amember of the peptidase T1A family, that is a 20S core alphasubunit. Alternative splicing results in multiple transcriptvariants encoding distinct isoforms.
Zhang, Y., et al. Biochem. Biophys. Res. Commun. 355(1):245-251(2007)Apcher, G.S., et al. FEBS Lett. 569 (1-3), 211-216 (2004) :Jayarapu, K., et al. Biochem. Biophys. Res. Commun. 314(2):523-528(2004)Apcher, G.S., et al. FEBS Lett. 553 (1-2), 200-204 (2003) :Huang, X., et al. J. Mol. Biol. 323(4):771-782(2002)
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