GUCY1A3抗体—艾普蒂

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     Black line: Control Antigen (100 ng); Purple line: Antigen(10ng); Blue line: Antigen (50 ng); Red line: Antigen (100 ng);    

  
  

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     Western blot analysis using GUCY1A3 mouse mAb against HEK293 (1) and Raji (2) cell lysate.    

  
  

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     Immunofluorescence analysis of HepG2 cells using GUCY1A3 mouse mAb (green). Blue: DRAQ5 fluorescent DNA dye.    

  
  

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     Flow cytometric analysis of HEK293 cells using GUCY1A3 mouse mAb (green) and negative control (purple).    

  
  

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     Immunohistochemical analysis of paraffin-embedded human renal cancer tissues using GUCY1A3 mouse mAb with DAB staining.    

  
  

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     Immunohistochemical analysis of paraffin-embedded human esophageal cancer tissues using GUCY1A3 mouse mAb with DAB staining.    

  
  

The GUCY1A3 antibody targets the GUCY1A3 protein, a key subunit of the soluble guanylate cyclase (sGC) enzyme. sGC, composed of α (GUCY1A3) and β (GUCY1B1) subunits, mediates nitric oxide (NO) signaling by converting GTP to cyclic guanosine monophosphate (cGMP), a critical secondary messenger regulating vascular tone, platelet function, and smooth muscle relaxation. GUCY1A3 is particularly vital in cardiovascular physiology, influencing blood pressure homeostasis and endothelial function. Mutations or dysregulation in GUCY1A3 have been linked to hypertension, atherosclerosis, and coronary artery disease.

Antibodies against GUCY1A3 are essential tools for studying its expression, localization, and interaction partners in tissues or cell models. They enable detection via techniques like Western blotting, immunohistochemistry, and immunofluorescence, aiding research into sGC's role in disease mechanisms. Additionally, these antibodies support drug discovery efforts targeting the NO-sGC-cGMP pathway, a therapeutic focus for cardiovascular disorders. Recent studies also explore GUCY1A3's involvement in cancer and pulmonary hypertension, broadening its biomedical relevance.

Despite its importance, GUCY1A3's function can be context-dependent, influenced by oxidative stress or co-subunit availability, highlighting the need for specific, high-affinity antibodies to ensure accurate experimental outcomes.