CARMIL1抗体;CARMIL1 Antibody—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P13019(CARMIL1 Antibody) at dilution 1/35. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human tonsil tissue using P13019(CARMIL1 Antibody) at dilution 1/35. (Original magnification: ×200)    

  
  

CARMIL1 (Capping Protein Arp2/3 Myosin-I Linker 1), also known as LRRC16A, is a multidomain scaffold protein involved in regulating actin cytoskeleton dynamics and membrane trafficking. It interacts with capping protein (CPαβ), which controls actin filament elongation, and modulates the activity of the Arp2/3 complex, a key driver of branched actin networks. CARMIL1 contains leucine-rich repeats (LRR), a C1 domain, and a CARMIL-specific homology (CSH) domain, enabling interactions with signaling molecules, membrane lipids, and cytoskeletal components. Its role in linking myosin-I motors to actin networks highlights its importance in cellular processes like cell migration, endocytosis, and cytokinesis.

CARMIL1 antibodies are essential tools for studying its expression, localization, and molecular interactions. They are widely used in techniques such as Western blotting, immunofluorescence, and immunoprecipitation to investigate CARMIL1's regulatory functions in actin remodeling and membrane trafficking pathways. Dysregulation of CARMIL1 has been implicated in diseases, including cancer and immune disorders, making its antibodies valuable for exploring pathological mechanisms. Recent studies also suggest CARMIL1's involvement in T-cell activation and lysosomal positioning, emphasizing its broader role in cellular homeostasis. Researchers often validate antibody specificity using knockout cell lines or siRNA knockdown to ensure accurate detection in diverse experimental models.