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     The image is immunohistochemistry of paraffin-embedded Human colorectal cancer tissue using P13119(DNAJC2 Antibody) at dilution 1/35. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human ovarian cancer tissue using P13119(DNAJC2 Antibody) at dilution 1/35. (Original magnification: ×200)    

  
  

The DNAJC2 antibody targets the DNAJC2 protein, a member of the evolutionarily conserved J-domain protein (JDP) family, which functions as co-chaperones for heat shock protein 70 (HSP70). DNAJC2. also known as HSPF2 or MIDA1. plays a critical role in protein folding, quality control, and cellular stress responses. Structurally, it contains a J-domain that facilitates interaction with HSP70. along with zinc finger motifs and nuclear localization signals, enabling its involvement in transcriptional regulation and chromatin remodeling. DNAJC2 is ubiquitously expressed and localizes to both the cytoplasm and nucleus, participating in diverse processes such as ribosome biogenesis, mRNA stability, and apoptosis.

Antibodies against DNAJC2 are widely used in research to study its expression patterns, subcellular localization, and interactions with partner proteins like STIP1 or HSP70. These tools are essential for elucidating DNAJC2's role in diseases, including cancer, where its overexpression correlates with tumor progression and chemoresistance, and neurodegenerative disorders linked to protein misfolding. DNAJC2 antibodies are validated for techniques such as Western blotting, immunoprecipitation, and immunofluorescence, aiding in mechanistic studies of its chaperone functions and regulatory networks. Ongoing research focuses on its potential as a therapeutic target or biomarker in conditions involving proteostasis imbalance.