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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 ANXA5 mouse mAb against PANC-1 (1), Hela (2), A431 (3), A549 (4) and MCF-7 (5) cell lysate.    

  
  

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     Flow cytometric analysis of Hela cells using ANXA5 mouse mAb (green) and negative control (red).    

  
  

SERPINB6. a member of the serine protease inhibitor (serpin) superfamily, is an intracellular protein that regulates proteolytic activity by inhibiting specific serine and cysteine proteases. It belongs to the clade B serpins, which are characterized by their cytoplasmic or nuclear localization. SERPINB6 primarily targets proteases such as cathepsin G and neutrophil elastase, playing a role in maintaining cellular homeostasis, preventing excessive proteolysis, and modulating inflammatory responses. Its expression is observed in various tissues, including the epidermis, inner ear, and platelets, implicating its involvement in diverse physiological processes.

Antibodies against SERPINB6 are essential tools for studying its expression, localization, and function in both normal and pathological contexts. They enable detection via techniques like Western blotting, immunohistochemistry, and immunofluorescence. Research using these antibodies has linked SERPINB6 dysregulation to several conditions, such as sensorineural hearing loss (due to its role in cochlear function), skin disorders, and cancer. For instance, reduced SERPINB6 levels in tumors may correlate with enhanced protease activity and metastasis. Both monoclonal and polyclonal SERPINB6 antibodies are available, with applications ranging from basic research to potential diagnostic or therapeutic development. Their specificity and validation remain critical for ensuring accurate interpretation in studies exploring SERPINB6's biological and clinical significance.