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     Western blot analysis using WWP2 mouse mAb against  Jurkat lysate    

  
  

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     Lane 1: Jurkat lysate;  Lane 2: WWP2 immunoprecipitated from Jurkat lysate by P15769;  Lane 3: The same as Lane 2 but use IgG isotype control antibody ;Result: P15769 can immunoprecipitate WWP2;    

  
  

The WWP2 antibody is a crucial tool for studying the biological functions of WWP2 (WW Domain-Containing E3 Ubiquitin Protein Ligase 2), a member of the NEDD4 family of HECT-type E3 ubiquitin ligases. WWP2 regulates protein stability and signaling pathways by catalyzing ubiquitination, a post-translational modification that tags substrates for proteasomal degradation or functional modulation. Structurally, WWP2 contains a C2 domain (for membrane binding), multiple WW domains (mediating protein-protein interactions), and a catalytic HECT domain. It interacts with key targets such as PTEN, SMADs, and RUNX2. impacting processes like cell growth, differentiation, and cancer progression. Dysregulation of WWP2 is linked to tumorigenesis, bone disorders, and neurodegenerative diseases. For instance, WWP2 overexpression in certain cancers promotes oncogenic signaling, while its loss may impair bone development.

WWP2 antibodies enable researchers to detect and quantify WWP2 expression in cells and tissues via techniques like Western blotting, immunohistochemistry, and immunofluorescence. They also facilitate functional studies, such as co-immunoprecipitation to identify binding partners or assess ubiquitination activity. Commercial antibodies vary in specificity, host species (e.g., rabbit, mouse), and clonality (monoclonal/polyclonal), requiring validation for target applications. Recent studies emphasize the antibody's role in exploring WWP2's dual roles in cancer—acting as both oncogene and tumor suppressor, depending on context—and its therapeutic potential as a drug target. Proper controls (e.g., knockout validation) are essential to ensure antibody reliability in experimental settings.