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     Western blot analysis of GYPB (arrow) using rabbit polyclonal GYPB Antibody (Center) (Cat. #P31325). 293 cell lysates (2 ug/lane) either nontransfected (Lane 1) or transiently transfected (Lane 2) with the GYPB gene.    

  
  

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     GYPB Antibody (Center) (Cat. #P31325)immunohistochemistry analysis in formalin fixed and paraffin embedded human liver tissue followed by peroxidase conjugation of the secondary antibody and DAB staining.This data demonstrates the use of GYPB Antibody (Center) for immunohistochemistry.  Clinical relevance has not been evaluated.    

  
  

UGGT1 (UDP-glucose:glycoprotein glucosyltransferase 1) is an endoplasmic reticulum (ER)-resident enzyme central to glycoprotein quality control. It acts as a folding sensor in the calnexin/calreticulin chaperone cycle, selectively recognizing misfolded or incompletely assembled N-glycosylated proteins. UGGT1 catalyzes the reglucosylation of exposed hydrophobic regions on these glycoproteins, tagging them with a glucose moiety. This glucose signal allows the proteins to rebind calnexin/calreticulin, granting additional opportunities for proper folding while preventing premature ER exit.

Antibodies targeting UGGT1 are valuable tools for studying ER-associated protein folding mechanisms and stress responses. Researchers use these antibodies in techniques like Western blotting, immunofluorescence, and immunoprecipitation to analyze UGGT1 expression levels, subcellular localization, and interactions with client proteins or chaperones. They are particularly relevant in disease research, as UGGT1 dysfunction has been implicated in neurodegenerative disorders (e.g., Parkinson’s and Alzheimer’s diseases), cancer progression (via modulation of oncogenic glycoproteins), and diabetes (linked to insulin processing). Validated UGGT1 antibodies help investigate how ER stress pathways, such as the unfolded protein response (UPR), adapt to folding challenges. Commercial antibodies are typically raised against specific epitopes, with validation data confirming reactivity across human, mouse, and rat models. These reagents continue to advance our understanding of proteostasis networks and therapeutic strategies targeting protein-misfolding pathologies.