Proteasome Marker Antibodies
The proteasome is a large multi-protein complex that serves to degrade damaged or unneeded proteins in a cell by proteolysis. Every proteasome is made up of four stacked rings that form a central core where proteins are degraded. Each of the four rings contains seven subunits. The two inner rings consist of seven beta subunits that are primarily catalytic. The two outer rings are made up of seven alpha subunits which form the entrance to the core. These alpha subunits are structural and function as a gate to block unregulated entrance to the interior. They also contain docking domains for regulatory particles.
Proteasomal degradation is critical to many cellular processes including cellular metabolism, heat shock and stress response, antigen presentation, modulation of cell surface receptors and ion channels, cell cycle regulation, transcription, and signaling factors. Several genetic diseases are associated with defects in the ubiquitin-proteasome pathway. Some examples of affected proteins include those linked to cystic fibrosis, Angelman’s syndrome, and Liddle syndrome.
Proteasome marker antibodies detect proteins specific to the proteasome and can aid in the study of the structure and dynamics of the proteasome. Proteasome marker antibodies can also help elucidate the role or roles a protein may play in a number of tasks that are centered in or influenced by the proteasomes. Quality Invitrogen proteasome marker antibodies are available for a variety of research needs.
Proteasome marker antibody targets
Featured product data
Immunofluorescent analysis of proteasome 20S X (green) showing staining in the cytoplasm and nucleus of Hela cells (right) compared to a negative control without primary antibody (left). Formalin-fixed cells were permeabilized with 0.1% Triton X-100 in TBS for 5–10 minutes and blocked with 3% BSA-PBS for 30 minutes at room temperature. Cells were probed with a proteasome 20S X polyclonal antibody (Cat. No. PA1-977) in 3% BSA-PBS at a dilution of 1:100 and incubated overnight at 4°C in a humidified chamber. Cells were washed with PBST and incubated with a DyLight 488-conjugated secondary antibody (Cat. No. 35553) in PBS at room temperature in the dark. F-actin (red) was stained with red-fluorescent phalloidin, and nuclei (blue) were stained with Hoechst or DAPI dye. Images were taken at a magnification of 60x.
Annotated product references
Cat. No. PA1-972 was used in western blot to investigate the mechanism for glucosamine-induced cell apoptosis in cancer cells. Experimental & molecular medicine (Sep 2011; 43: 487) "Glucosamine induces cell death via proteasome inhibition in human ALVA41 prostate cancer cell." Liu BQ,Meng X,Li C,Gao YY,Li N,Niu XF,Guan Y,Wang HQ
Cat. No. PA1-977 was used in western blot to study the role of immunoproteasome subunit LMP2 in apoptosis of PC-3 cells and tumor growth in nude mice. British journal of cancer (Jun 2012; 107: 53) A selective inhibitor of the immunoproteasome subunit LMP2 induces apoptosis in PC-3 cells and suppresses tumour growth in nude mice." Wehenkel M,Ban JO,Ho YK,Carmony KC,Hong JT,Kim KB
For Research Use Only. Not for use in diagnostic procedures.