Rabbit Polyclonal PSMD3 Antibody

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     All lanes : Anti-PSMD3 Antibody (C-Term) at 1:2000 dilution Lane 1: Jurkat whole cell lysate Lane 2: Hela whole cell lysate Lane 3: HepG2 whole cell lysate Lane 4: MCF-7 whole cell lysate Lane 5: NIH/3T3 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG,  (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 61 kDa Blocking/Dilution buffer: 5% NFDM/TBST.    

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     Overlay histogram showing HeLa cells stained with P34443(green line).  The cells were fixed with 2% paraformaldehyde (10 min) and then permeabilized with 90% methanol for 10 min.  The cells were then icubated in 2% bovine serum albumin to block non-specific protein-protein interactions followed by the antibody (P34443,  1:25 dilution) for 60 min at 37ºC.  The secondary antibody used was Goat-Anti-Rabbit IgG, DyLight® 488 Conjugated Highly Cross-Adsorbed(OE188374) at 1/200 dilution for 40 min at 37ºC.  Isotype control antibody (blue line) was rabbit IgG1 (1μg/1x10^6 cells) used under the same conditions.  Acquisition of >10, 000 events was performed.    

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     P34443 staining PSMD3 in human brain tissue sections by Immunohistochemistry (IHC-P - paraformaldehyde-fixed,  paraffin-embedded sections).  Samples were incubated with primary antibody (1/250) for 1 hours at room temperature.  A undiluted biotinylated goat polyvalent antibody was used as the secondary antibody.    

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     P34443 staining PSMD3  in human testis tissue sections by Immunohistochemistry (IHC-P - paraformaldehyde-fixed,  paraffin-embedded sections).  Samples were incubated with primary antibody (1/250) for 1 hours at room temperature.  A undiluted biotinylated goat polyvalent antibody was used as the secondary antibody.    

The PSMD3 (Proteasome 26S Subunit, Non-ATPase 3) antibody is a tool used to study the 26S proteasome, a large multi-subunit complex critical for protein degradation in eukaryotic cells. PSMD3. also known as Rpn3. is a component of the 19S regulatory particle of the 26S proteasome, which recognizes ubiquitinated proteins and facilitates their ATP-dependent unfolding and translocation into the proteolytic core (20S particle). This subunit plays a role in maintaining proteasome stability and regulating substrate specificity.

Antibodies targeting PSMD3 are essential for investigating proteasome structure, function, and dynamics in cellular processes like protein quality control, cell cycle regulation, and stress responses. They are widely employed in techniques such as Western blotting, immunoprecipitation, and immunofluorescence to detect PSMD3 expression, localization, and interactions. Dysregulation of PSMD3 has been implicated in diseases including cancer, neurodegenerative disorders, and autoimmune conditions, making its study relevant for therapeutic development.

Commercial PSMD3 antibodies are typically raised in rabbits or mice using peptide immunogens derived from conserved regions of the human protein. Validation often includes testing for specificity via knockdown/knockout controls and cross-reactivity assessments. Researchers utilize these antibodies to explore proteasome dysfunction mechanisms or evaluate experimental inhibitors targeting the ubiquitin-proteasome system for disease treatment.