WIPI2抗体—艾普蒂

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     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane 1-2: Human lung tissue and Human placenta tissue lysates, Primary antibody: P06002(WIPI2 Antibody) at dilution 1/300, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 2 minutes    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P06002(WIPI2 Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human brain tissue using P06002(WIPI2 Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

WIPI2 (WD repeat domain phosphoinositide-interacting protein 2) is a key regulator of autophagy, a cellular degradation process critical for maintaining homeostasis. Belonging to the WIPI protein family, it contains seven WD40 repeats that facilitate protein-protein interactions and a conserved motif for binding phosphatidylinositol 3-phosphate (PI3P). WIPI2 is primarily involved in the early stages of autophagosome formation, where it localizes to omegasomes – PI3P-rich subdomains of the endoplasmic reticulum.

Functionally, WIPI2 acts as a scaffold protein, recruiting downstream effectors like ATG16L1 to initiate LC3 lipidation, a process essential for autophagosome membrane expansion. Its role in connecting phosphoinositide signaling to autophagic machinery makes it vital for both canonical autophagy and selective autophagy pathways. Dysregulation of WIPI2 has been linked to neurodegenerative diseases, cancer, and immune disorders, reflecting autophagy's broad physiological impact.

WIPI2 antibodies are widely used tools in autophagy research, enabling detection of endogenous WIPI2 expression through techniques like immunoblotting, immunofluorescence, and immunohistochemistry. Specific antibodies targeting distinct isoforms (WIPI2A and WIPI2B) help elucidate isoform-specific functions. These reagents are crucial for studying autophagy dynamics, protein localization, and molecular mechanisms in disease models, making them indispensable for both basic research and therapeutic development targeting autophagy-related pathologies.