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     The image is immunohistochemistry of paraffin-embedded Human esophagus cancer tissue using P08894(TEP1 Antibody) at dilution 1/190. (Original magnification: ×200)    

  
  

TEP1 (Telomerase-associated protein 1), also known as TERC-binding protein, is a critical component of the telomerase complex, which plays a pivotal role in maintaining telomere integrity and cellular immortality. Telomerase counteracts telomere shortening during DNA replication by adding repetitive nucleotide sequences to chromosome ends. The TEP1 protein interacts with the telomerase RNA component (TERC) and the catalytic subunit TERT (telomerase reverse transcriptase), stabilizing the complex and facilitating its nuclear localization and enzymatic activity. While TEP1 is not directly involved in the catalytic function of telomerase, it is essential for telomerase assembly and RNA binding.

Antibodies targeting TEP1 are widely used in research to investigate telomerase biology, particularly in studies related to aging, cancer, and stem cell regulation. These antibodies enable the detection and quantification of TEP1 expression in various tissues and cell types through techniques like Western blotting, immunoprecipitation, and immunofluorescence. Dysregulation of TEP1 has been implicated in telomerase-deficient disorders and oncogenesis, making it a biomarker of interest in cancer diagnostics and therapeutic development. Notably, TEP1 homologs are evolutionarily conserved across species, underscoring its fundamental role in telomere maintenance. Research using TEP1 antibodies continues to elucidate its molecular interactions and potential clinical applications in age-related diseases and malignancies.