Grp75抗体;Grp75 Antibody—艾普蒂

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     Western blot analysis of Grp75 expression in (1) HeLa cell lysate; (2) Mouse liver lysate.    

  
  

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     All lanes use the Antibody at 1:2K dilution for 1 hour at room temperature.    

  
  

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     All lanes use the Antibody at 1:2K dilution for 1 hour at room temperature.    

  
  

Grp75. also known as glucose-regulated protein 75 (GRP75), mortalin, or HSPA9. is a member of the heat shock protein 70 (HSP70) family. It is a multifunctional chaperone protein primarily localized in mitochondria, where it facilitates mitochondrial protein import, quality control, and energy metabolism. Additionally, Grp75 is found in the endoplasmic reticulum (ER) and cytosol, participating in cellular stress responses, anti-apoptotic signaling, and calcium homeostasis by bridging the mitochondria-associated ER membrane (MAM). Its interaction with the inositol 1.4.5-trisphosphate receptor (IP3R) regulates ER-mitochondrial Ca²⁺ transfer, influencing cell survival and death pathways.

Grp75 antibodies are essential tools for studying its expression, localization, and functional roles in both physiological and pathological contexts. These antibodies are widely used in techniques like Western blotting, immunohistochemistry (IHC), and immunoprecipitation (IP) to detect Grp75 in various tissues and cell types. Commercially available Grp75 antibodies are often raised against specific epitopes, with host species (e.g., rabbit, mouse) and clonal types (monoclonal/polyclonal) varying by supplier. Researchers utilize these antibodies to explore Grp75's involvement in diseases such as cancer (where it is overexpressed and linked to tumor progression and chemoresistance) and neurodegenerative disorders (e.g., Alzheimer’s and Parkinson’s diseases, where it interacts with misfolded proteins like β-amyloid and α-synuclein). Validation of antibody specificity through knockout controls or siRNA knockdown is critical to ensure accurate experimental outcomes.