ATP6V1E2抗体—艾普蒂

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     Gel: 12%SDS-PAGE, Lysate: 40 μg, Lane 1-3: TM4 cell, Hela cell, Mouse brain tissue lysates, Primary antibody: P09178(ATP6V1E2 Antibody) at dilution 1/450, Secondary antibody: Goat anti rabbit IgG at 1/5000 dilution, Exposure time: 1 minute    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P09178(ATP6V1E2 Antibody) at dilution 1/120. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human colorectal cancer tissue using P09178(ATP6V1E2 Antibody) at dilution 1/120. (Original magnification: ×200)    

  
  

The ATP6V1E2 antibody targets the ATP6V1E2 protein, a subunit of the vacuolar-type H+-translocating ATPase (V-ATPase) complex, which plays a critical role in regulating intracellular pH and membrane trafficking. V-ATPases are multisubunit proton pumps that acidify organelles like lysosomes, endosomes, and secretory vesicles, influencing processes such as protein degradation, ion homeostasis, and neurotransmitter release. The ATP6V1E2 subunit, part of the V1 domain, is involved in ATP hydrolysis and proton translocation. While the ubiquitously expressed ATP6V1E1 is well-characterized, ATP6V1E2 is a less-studied isoform with tissue-specific expression, notably in the kidney, testis, and certain cancer cells.

Antibodies against ATP6V1E2 are primarily used in research to investigate its physiological roles and dysregulation in diseases. Studies suggest ATP6V1E2 may contribute to renal tubular acidosis, neurodegenerative disorders, and tumor progression, where altered V-ATPase activity affects microenvironment acidity and cell survival. These antibodies enable detection via techniques like Western blotting, immunohistochemistry, and immunofluorescence, aiding in protein localization and expression analysis. Commercial ATP6V1E2 antibodies are typically raised in rabbits or mice, validated for specificity using knockout controls. Their development supports ongoing exploration of V-ATPase diversity and isoform-specific functions, offering insights into therapeutic targeting for conditions linked to pH dysregulation.