MTBP (Mdm2-binding protein) is a multifunctional protein first identified through its interaction with Mdm2. a key negative regulator of the tumor suppressor p53. Discovered in the early 2000s, MTBP plays roles in cell cycle regulation, DNA replication stress response, and oncogenesis. Structurally, it contains an Mdm2-binding domain and a conserved N-terminal domain involved in protein interactions. MTBP facilitates Mdm2-mediated degradation of p53. linking it to p53-dependent tumor suppression. However, studies also highlight p53-independent functions, including modulation of the Akt/mTOR and Hippo signaling pathways, influencing cell proliferation, migration, and metastasis.
MTBP’s dual role in cancer remains context-dependent: it exhibits oncogenic properties in certain cancers (e.g., breast, lung) by promoting cell survival and invasion, while acting as a tumor suppressor in others (e.g., melanoma). This complexity drives interest in MTBP antibodies as research tools to study its expression, localization, and interactions in cancer models. Commercial MTBP antibodies are widely used in techniques like Western blot, immunohistochemistry, and immunofluorescence to explore its diagnostic or therapeutic potential.
Current research focuses on clarifying MTBP’s mechanistic roles in replication stress, metastasis, and therapy resistance, with antibodies critical for validating its clinical relevance as a biomarker or target. Challenges include resolving isoform-specific functions and optimizing antibody specificity across diverse experimental systems.