MYCBP抗体—艾普蒂

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     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P10612(MYCBP Antibody) at dilution 1/70. (Original magnification: ×200)    

  
  

MYCBP (MYC-binding protein), also known as PHR (Pam/Highwire/RPM-1), is a conserved E3 ubiquitin ligase implicated in diverse cellular processes, including neuronal development, cancer progression, and immune regulation. Initially identified as a binding partner of the MYC oncoprotein, MYCBP regulates MYC protein stability by promoting its ubiquitination and proteasomal degradation, thereby modulating MYC-driven transcriptional programs critical for cell proliferation and apoptosis. Structurally, MYCBP contains a characteristic N-terminal RING-H2 domain essential for its E3 ligase activity and a C-terminal region involved in protein-protein interactions.

Beyond MYC regulation, MYCBP plays pivotal roles in neural development by controlling axon guidance, synapse formation, and synaptic plasticity through interactions with signaling pathways like mTOR and MAPK. In cancer, MYCBP dysregulation is linked to tumorigenesis, metastasis, and chemoresistance, with overexpression observed in multiple malignancies. Its involvement in immune responses, particularly in T-cell activation and inflammatory signaling, further underscores its functional versatility.

MYCBP antibodies are widely used in research to study protein expression, localization, and interactions via techniques such as Western blotting, immunoprecipitation, and immunofluorescence. They are valuable tools for exploring MYCBP's dual roles in physiological homeostasis and disease pathogenesis, offering potential insights into therapeutic targeting of MYC-associated cancers or neurodevelopmental disorders. Ongoing studies continue to unravel its complex regulatory networks across tissues and pathologies.