TRIP6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 TRIP6 mouse mAb against K562 and A431 (2) cell lysate.    

  
  

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     Flow cytometric analysis of K562 cells using TRIP6 mouse mAb (green) and negative control (red).    

  
  

TRIP6 (Thyroid Receptor Interacting Protein 6), also known as OIP-1 or ZRP-1. is a member of the zyxin family of LIM domain-containing proteins. It functions as a scaffold or adaptor protein involved in diverse cellular processes, including cell adhesion, migration, signaling transduction, and transcriptional regulation. TRIP6 localizes to focal adhesions, cell-cell junctions, and the nucleus, interacting with multiple partners such as integrins, receptor tyrosine kinases, and transcription factors (e.g., NF-κB, AP-1). It plays roles in cytoskeletal remodeling, mechanotransduction, and pathways like Hippo/YAP, Wnt, and TGF-β. Dysregulation of TRIP6 is implicated in cancer progression, metastasis, and therapy resistance, particularly in breast, lung, and gastric cancers, where it often promotes proliferation, invasion, and survival.

TRIP6 antibodies are essential tools for detecting TRIP6 expression, localization, and post-translational modifications in techniques like Western blotting, immunofluorescence, and immunohistochemistry. They aid in studying its molecular functions, interactions, and disease associations. Commercial TRIP6 antibodies are typically raised against specific epitopes (e.g., N-terminal or LIM domains) and validated for species reactivity (human, mouse, rat). Researchers use these antibodies to explore TRIP6’s role in cancer biology, mechanobiology, and potential therapeutic targeting. Validation via knockout/knockdown controls is critical due to occasional cross-reactivity with homologous zyxin family members.