HSC70InteractingProteinHIP抗体;HSC70InteractingProteinHIP Antibody—艾普蒂 新品

+ +

•  

   

     Western blot analysis of HSC70 Interacting Protein HIP expression in 293T cell lysate.    

  
  

•  

   

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

  
  

•  

   

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

  
  

The HSC70-interacting protein (HIP), also known as ST13. is a co-chaperone that binds to the ATPase domain of HSC70/HSP70. stabilizing its ADP-bound state to regulate substrate binding and release during protein folding and trafficking. HIP plays a critical role in the chaperone-mediated autophagy (CMA) pathway, facilitating the selective degradation of cytosolic proteins by lysosomes. It is involved in stress response, protein quality control, and cellular homeostasis, with implications in cancer, neurodegenerative diseases, and aging.

Antibodies targeting HIP are widely used to study its expression, localization, and interaction networks in cellular models and tissues. These antibodies enable researchers to explore HIP's role in modulating HSC70 activity, its participation in CMA under stress conditions (e.g., oxidative stress, nutrient deprivation), and its dysregulation in pathologies such as Alzheimer's disease, Parkinson's disease, and various cancers. For instance, reduced HIP levels have been linked to impaired CMA in neurodegenerative disorders, while its overexpression in certain tumors correlates with metastasis and drug resistance.

Commercial HIP antibodies are typically developed in hosts like rabbits or mice, validated for applications including Western blotting, immunoprecipitation, and immunofluorescence. Specificity is confirmed using knockout controls or siRNA-mediated knockdown. Ongoing research focuses on HIP as a potential therapeutic target or biomarker, driving demand for reliable antibodies to dissect its molecular mechanisms in health and disease.