HSP90B1抗体

+ +

•  

   

     Gel: 10%SDS-PAGE, Lysate: 40 μg, Lane 1-4: Hela cells, human liver cancer tissue, Jurkat cells, NIH/3T3 cells, Primary antibody: P07331(HSP90B1 Antibody) at dilution 1/900, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 3 seconds    

  
  

•  

   

     The image is immunohistochemistry of paraffin-embedded Human brain tissue using P07331(HSP90B1 Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

•  

   

     The image is immunohistochemistry of paraffin-embedded Human ovarian cancer tissue using P07331(HSP90B1 Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

HSP90B1. also known as GRP94 or endoplasmin, is a member of the heat shock protein 90 (HSP90) family, functioning as a molecular chaperone in the endoplasmic reticulum (ER). It plays a critical role in protein folding, quality control, and the regulation of ER stress responses by binding to nascent glycoproteins and ensuring proper conformation. Unlike its cytosolic counterparts (HSP90α and HSP90β), HSP90B1 is ER-resident and participates in the unfolded protein response (UPR), making it essential for maintaining cellular homeostasis under stress conditions.

Antibodies targeting HSP90B1 are widely used in research to study its expression, localization, and interaction networks. These antibodies enable detection via techniques like Western blotting, immunofluorescence, and immunohistochemistry, aiding investigations into diseases linked to ER dysfunction, such as cancer, neurodegenerative disorders, and diabetes. In cancer biology, HSP90B1 is implicated in tumor progression, metastasis, and drug resistance due to its role in stabilizing oncogenic clients and modulating immune surveillance. Its selective inhibition has emerged as a therapeutic strategy, driving demand for specific antibodies to validate target engagement in preclinical models.

Researchers also utilize HSP90B1 antibodies to explore its immunoregulatory functions, including antigen presentation pathways. However, cross-reactivity with other HSP90 isoforms remains a challenge, emphasizing the need for rigorous antibody validation using knockout controls or epitope mapping.