SWAP70抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human brain tissue using P08950(SWAP70 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human colorectal cancer tissue using P08950(SWAP70 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

SWAP70 (Switching B-cell complex 70 kDa subunit) is a unique signaling protein involved in B-cell antigen receptor signaling, immune regulation, and cytoskeletal dynamics. Discovered in 2000. it belongs to the SAC (SWAP-ACD) family and contains a pleckstrin homology (PH) domain for membrane binding and a SWAP domain mediating protein interactions. It regulates PI3K-Akt signaling, membrane ruffling, and cell migration in immune cells (B cells, dendritic cells) and epithelial cells.

SWAP70 antibodies are critical tools for studying its role in immune responses, inflammation, and autoimmune diseases (e.g., rheumatoid arthritis, allergies). They enable detection of SWAP70 expression, localization (cytosolic-to-membrane translocation upon activation), and interactions via techniques like Western blot, immunofluorescence, and flow cytometry. Research using these antibodies has linked SWAP70 dysfunction to cancer metastasis, immunodeficiency, and abnormal T-cell/B-cell activation. Commercial SWAP70 antibodies are typically raised against specific epitopes (human/mouse) and validated for cross-reactivity. Their applications span mechanistic studies of immune signaling, validation of SWAP70 knockout models, and clinical research exploring SWAP70 as a biomarker or therapeutic target.