Detection of Human LMP7/PSMB8 by Western Blot. Western blot shows lysates of MOLT‑4 human acute lymphoblastic leukemia cell line and Raji human Burkitt's lymphoma cell line. PVDF membrane was probed with 2 µg/mL of Mouse Anti-Human LMP7/|
PSMB8 Monoclonal Antibody (Catalog # MAB7710) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for LMP7/PSMB8 at approximately 23 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
PSMB8 (Proteasome Subunit beta type-8; Also beta 5i, RING10/Y2 and LMP7) is a 23-24 kDa member of the peptidase T1B family of molecules. It is expressed both constitutively and inducibly by IFN-gamma in a wide variety of cells, including immature dendritic cells, preadipocytes, CD4+ T cells and monocytes. LMP7 is a subunit of the 700 kDa, 20S proteasome catalytic complex, a dynamic intracellular structure that participates in ATP-dependent proteolytic activity. LMP7 qualifies as a beta -type, i (immuno)-type proteasome, meaning it both plays a chymotrypsin-like role in the turnover of proteins and is found in cytokine-responsive cells. The peptides generated through LMP7 activity are presented as antigens by MHC-I molecules. LMP7 activity is dependent upon the removal of the LMP7 precursor prosequence, an action that exposes a critical internal Thr residue. Human LMP7 is synthesized as a 28-29 kDa, 276 amino acid (aa) proprecursor. It contains a 72 aa autocleavable propeptide plus a 204 aa mature region. There is one alternative splice form that shows a 45 aa substitution for aa 1-49. This isoform does not appear to participate in formation of a proteosome. Over aa 73-276, human LMP7 shares 92% aa sequence identity with mouse LMP7.
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