DUSP9抗体—艾普蒂

+ +

•  

   

     The image is immunohistochemistry of paraffin-embedded Human prostate cancer tissue using P05654(DUSP9 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

•  

   

     The image is immunohistochemistry of paraffin-embedded Human ovarian cancer tissue using P05654(DUSP9 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

The dual-specificity phosphatase 9 (DUSP9), also known as MAP kinase phosphatase 4 (MKP-4), is a member of the dual-specificity phosphatase family that regulates mitogen-activated protein kinase (MAPK) signaling pathways. DUSP9 specifically dephosphorylates and inactivates extracellular signal-regulated kinase (ERK), p38. and c-Jun N-terminal kinase (JNK), thereby modulating cellular responses to stress, growth factors, and cytokines. It is primarily expressed in placental, kidney, and liver tissues, and has been implicated in embryonic development, glucose metabolism, and cancer progression.

DUSP9 antibodies are essential tools for studying its expression, localization, and function in physiological and pathological contexts. These antibodies enable detection of DUSP9 protein levels via techniques like Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF). Researchers utilize them to explore DUSP9's role in regulating MAPK signaling cascades, particularly in disorders such as diabetes, obesity, and certain malignancies. For instance, studies highlight DUSP9's involvement in insulin signaling and its potential as a therapeutic target for metabolic syndromes.

High-quality DUSP9 antibodies are validated for specificity, often through knockout cell line controls, ensuring reliable experimental outcomes. Commercial antibodies are typically raised in rabbits or mice, targeting specific epitopes within the conserved N-terminal or catalytic domains. Understanding DUSP9's regulatory mechanisms through antibody-based assays advances insights into cellular homeostasis and disease pathways.