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cellular roles and mechanisms of PI31 in regulation of proteasome function remain unclear and require future definition.
a model for FP domain-mediated dimerization of SCF (Montrer KITLG Protéines)(Fbxo7 (Montrer FBXO7 Protéines)) and PI31
PI31 acts as a selective modulator of the proteasome-mediated steps in MHC class I antigen processing
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 non-identical 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 non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a protein that inhibits the activation of the proteasome by the 11S and 19S regulators. Alternative transcript variants have been identified for this gene.
, proteasome inhibitor PI31 subunit
, proteasome inhibitor hP131 subunit
, proteasome inhibitor subunit 1
, proteasome (prosome, macropain) inhibitor subunit 1 (PI31)
, proteasome (prosome, macropain) inhibitor subunit 1