HSPA13抗体—艾普蒂

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     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane: Human uterus tissue lysate, Primary antibody: P10541(HSPA13 Antibody) at dilution 1/500, Secondary antibody: Goat anti rabbit IgG at 1/5000 dilution, Exposure time: 3 minutes    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human colorectal cancer tissue using P10541(HSPA13 Antibody) at dilution 1/90. (Original magnification: ×200)    

  
  

The HSPA13 antibody targets the heat shock protein family A (HSP70) member 13. a chaperone protein involved in cellular stress responses and protein homeostasis. HSPA13. also known as STCH or HSP70B′, is a member of the HSP70 family localized primarily in the endoplasmic reticulum (ER). Unlike other HSP70s, HSPA13 lacks an ATPase domain but retains substrate-binding capabilities, enabling participation in protein folding, degradation, and translocation. It plays roles in ER-associated degradation (ERAD), apoptosis regulation, and cellular adaptation to stressors like hypoxia or nutrient deprivation. Dysregulation of HSPA13 has been linked to cancer progression, neurodegenerative diseases, and immune disorders, highlighting its potential as a therapeutic target.

HSPA13 antibodies are critical tools for studying its expression, localization, and function. They are widely used in techniques such as Western blotting, immunohistochemistry (IHC), and immunofluorescence (IF) to assess protein levels in disease models or physiological conditions. These antibodies help elucidate HSPA13's interaction networks, post-translational modifications, and mechanistic contributions to stress adaptation. Commercial HSPA13 antibodies are typically validated for specificity against conserved epitopes, though cross-reactivity with other HSP70 members requires careful experimental controls. Research utilizing these antibodies continues to expand our understanding of HSPA13's role in cellular resilience and pathology.