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The 20S proteasome is a protease complex that is responsible for cytosolic protein degradation and generation of peptide ligands for major histocompatibility complex (MHC) class I molecules, either in their final form or in the form of amino-terminally extended precursors. Upon IFN-gamma stimulation of cells, three constitutively expressed subunits of the 20S proteasome are replaced by inducible subunits LMP2 (low-molecular mass polypeptide 2), LMP7, and MECL-1 (multicatalytic endopeptidase complex-like-1, LMP10). LMP2, LMP7, and MECL-1 subunits form immunoproteasomes, which are associated with more efficient class I antigen processing and presentation. Independent assortment of LMP-2, LMP-7, and MECL-1 into different proteasome complexes can lead to 36 unique proteasome subsets, which may mediate differences in the cleavage specificities/cleavage motifs of proteins subject to constitutive- and immuno-proteasomes.
beta2i; LMP10; Low molecular mass protein 10; macropain; Macropain subunit MECl-1; MECL1; Mecl-1; MGC1665; multicatalytic endopeptidase complex subunit MECl-1; OTTHUMP00000174858; prosome; prosome Mecl1; proteasome (prosome, macropain) subunit, beta type 10; proteasome (prosome, macropain) subunit, beta type, 10; proteasome (prosomome, macropain) subunit, beta type 10; proteasome 20S subunit beta 10; proteasome beta 10 subunit; proteasome catalytic subunit 2i; Proteasome MECl 1; proteasome MECl-1; proteasome subunit 10; proteasome subunit beta 10; proteasome subunit beta 7i; proteasome subunit beta type-10; Proteasome subunit beta-2i; proteasome subunit LMP10; proteasome subunit MECL1; PSMB 10; Psmb10
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