ADAM10抗体;ADAM10 Antibody—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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     Flow cytometric analysis of Hela cells using ADAM10 mouse mAb (green) and negative control (red).    

  
  

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     Flow cytometric analysis of THP-1 cells using ADAM10 mouse mAb (green) and negative control (red).    

  
  

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     Immunohistochemical analysis of paraffin-embedded human rectal cancer tissues using ADAM10 mouse mAb with DAB staining.    

  
  

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     Immunohistochemical analysis of paraffin-embedded human cervical cancer tissues using ADAM10 mouse mAb with DAB staining.    

  
  

ADAM10 (A Disintegrin and Metalloproteinase 10) is a transmembrane protease belonging to the ADAM family, which plays critical roles in ectodomain shedding of membrane-bound proteins. Initially identified in the 1990s, ADAM10 is involved in regulating key cellular processes such as cell adhesion, signaling, and proteolytic processing. Structurally, it contains a prodomain, catalytic metalloproteinase domain, disintegrin domain, cysteine-rich region, transmembrane domain, and cytoplasmic tail. Its sheddase activity targets substrates like Notch receptors, amyloid precursor protein (APP), E-cadherin, and growth factors, influencing pathways linked to development, immunity, and tissue homeostasis.

ADAM10’s dysregulation is implicated in pathologies including cancer, Alzheimer’s disease, and inflammatory disorders. For instance, its cleavage of APP contributes to amyloid-beta plaque formation in Alzheimer’s, while its role in Notch signaling affects tumor progression. Antibodies targeting ADAM10 are essential tools for studying its expression, localization, and function. They enable detection via techniques like Western blot, immunohistochemistry, and flow cytometry, with applications in both research and diagnostics. Some antibodies block enzymatic activity or substrate interactions, aiding mechanistic studies. Commercial ADAM10 antibodies vary in specificity, often validated against knockout models to confirm target selectivity. Challenges include distinguishing ADAM10 from homologous proteases (e.g., ADAM17) and ensuring epitope recognition across species. Ongoing research explores therapeutic modulation of ADAM10 activity, with antibodies serving as potential candidates for targeted inhibition in disease contexts.