CHERP抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P09497(CHERP Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P09497(CHERP Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

CHERP (Calcium Homeostasis Endoplasmic Reticulum Protein) is a ubiquitously expressed protein implicated in cellular calcium regulation and RNA splicing. Discovered in the early 2000s, it localizes to the endoplasmic reticulum (ER) and nucleus, reflecting its dual roles. In the ER, CHERP interacts with the sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2), modulating intracellular calcium homeostasis—a critical process for cell signaling, muscle contraction, and apoptosis. Simultaneously, nuclear CHERP participates in pre-mRNA splicing as a component of the spliceosome complex, influencing gene expression by regulating alternative splicing events.

CHERP’s involvement in calcium signaling links it to neurological and cardiovascular disorders, while its splicing function connects it to cancer progression and DNA damage response. Studies suggest CHERP depletion disrupts cell cycle progression and sensitizes cells to DNA-damaging agents, highlighting its potential role in genomic stability.

Antibodies targeting CHERP are essential tools for investigating its molecular mechanisms. They enable detection of CHERP expression via Western blot, immunofluorescence, and immunohistochemistry, aiding studies on its subcellular distribution and protein interactions. Such antibodies also facilitate research into CHERP’s pathological relevance, including its overexpression in certain cancers and its regulatory effects on calcium-dependent pathways. Development of specific, high-affinity anti-CHERP antibodies continues to support advancements in understanding cellular stress responses and disease pathogenesis.