UGGT2抗体—艾普蒂

+ +

•  

   

     The image is immunohistochemistry of paraffin-embedded Human prostate cancer tissue using P08939(UGGT2 Antibody) at dilution 1/25. (Original magnification: ×200)    

  
  

UGGT2 (UDP-glucose glycoprotein glucosyltransferase 2) is an endoplasmic reticulum (ER)-resident enzyme critical for quality control of N-linked glycoproteins. It acts as a key sensor in the ER-associated degradation (ERAD) pathway, selectively recognizing misfolded or incompletely folded glycoproteins. UGGT2 re-glucosylates exposed hydrophobic regions on these proteins, tagging them with a glucose residue to facilitate rebinding to calnexin/calreticulin chaperones for refolding attempts. If proper folding isn’t achieved, the protein is ultimately targeted for proteasomal degradation.

Antibodies against UGGT2 are essential tools for studying its expression, localization, and role in protein quality control mechanisms. They are widely used in Western blotting, immunofluorescence, and immunohistochemistry to investigate UGGT2's involvement in diseases linked to ER stress, such as neurodegenerative disorders, cancer, and metabolic syndromes. UGGT2-specific antibodies help distinguish it from its isoform UGGT1. which shares structural similarities but exhibits differences in substrate specificity and tissue distribution. Researchers also utilize these antibodies to explore UGGT2's interactions with other ERAD components or its dysregulation under pathological conditions, including viral infections and inflammatory responses. Validating antibody specificity is crucial due to sequence homology among glycosyltransferase family members. High-quality UGGT2 antibodies enable insights into cellular stress responses and potential therapeutic targets for protein-misfolding diseases.