N-myc (and STAT) interactor (NMI) is a protein initially identified through its interaction with N-myc and STAT signaling proteins, playing roles in transcriptional regulation and cellular signaling pathways. Discovered in the late 1990s, NMI is characterized by its coiled-coil domains, enabling interactions with key oncoproteins (e.g., c-myc, N-myc) and transcription factors (e.g., STATs). It modulates diverse processes, including cell proliferation, differentiation, apoptosis, and immune responses, particularly in interferon-γ signaling. Dysregulation of NMI expression has been implicated in cancers, such as breast cancer, glioblastoma, and neuroblastoma, where it may act as a tumor suppressor or oncogenic driver depending on context.
NMI antibodies are critical tools for studying its expression, localization, and function in both normal and pathological states. They enable detection via techniques like immunohistochemistry, Western blotting, and immunofluorescence, aiding research on NMI's role in cancer progression, immune regulation, and therapeutic resistance. However, challenges persist in antibody specificity due to NMI's structural homology with other proteins and variable splice isoforms. Recent studies also explore NMI's potential as a diagnostic or prognostic biomarker, emphasizing the need for validated antibodies to ensure experimental reproducibility. Ongoing research continues to unravel NMI's complex interactions and clinical relevance in disease mechanisms.