LMP2 Antibody (G-3) is a high quality monoclonal LMP2 antibody (also designated PSB9 antibody, Proteasome 20S Subunit Beta 9 antibody, PSMB6i antibody, RING12 antibody, Multicatalytic Endopeptidase Complex Chain 7 antibody, Really Interesting New Gene 12 Protein antibody, Large Multifunctional Peptidase 2 antibody, Proteasome Subunit Beta-1i antibody, Proteasome Subunit Beta 9 antibody, Proteasome Chain 7 antibody, Beta1i antibody, LMP2 antibody, Proteasome-Related Gene 2 antibody, Proteasome Subunit Β1i antibody, or PRAAS3 antibody) suitable for the detection of the LMP2 protein of mouse, rat and human origin. LMP2 Antibody (G-3) is available as both the non-conjugated anti-LMP2 antibody form, as well as multiple conjugated forms of anti-LMP2 antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. The eukaryotic multicatalytic proteinase complex, otherwise known as the proteasome, is present in both the nucleus and cytoplasm of cells and contains at least 15 nonidentical subunits, which form a highly ordered ring-shaped structure. The proteasome is involved in an ATP/Ubiquitin-dependent proteolytic pathway and expresses at least five distinct proteolytic activities, including the cleavage of peptides after branched chain amino acids or bulky hydrophobic amino acids. Two components of the proteasome are the low molecular mass proteins LMP2 and LMP7, which are thought to connect the proteasome to the MHC class-I antigen-processing pathway. Upon stimulation with IFN-γ, LMP2 and LMP7 displace housekeeping subunits in the proteasome and activate cytotoxic T cells (CTLs). LMP2 and LMP7 are produced as precursor proteins, which are processed to subunits that have the ability to complex with the proteasome. LMP2 is expressed as two alternatively spliced forms, LMP2.l and LMP2.s, in lymphoblastoid cell lines and in fibroblasts after IFN-γ stimulation. LMP7 is also expressed as two forms, LMP7-E1 and E2, in several tissues.
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