CABIN1 (Calcineurin-binding protein 1), also known as CAIN or CARP, is a ubiquitously expressed scaffolding protein that plays a critical role in regulating calcineurin, a calcium-dependent phosphatase involved in immune response, neuronal signaling, and cardiac hypertrophy. It contains multiple functional domains, including calcineurin-binding motifs, enabling it to suppress calcineurin/NFAT signaling pathways by directly inhibiting phosphatase activity or sequestering transcription factors. Dysregulation of CABIN1 is implicated in autoimmune diseases, cancer progression, and neurological disorders.
CABIN1 antibodies are essential tools for studying its expression, localization, and interaction networks. They are widely used in techniques like Western blotting, immunoprecipitation, and immunofluorescence to explore CABIN1's role in T-cell activation, apoptosis, and epigenetic regulation (via association with histone deacetylases). Researchers also utilize these antibodies to investigate CABIN1's tumor-suppressive functions, as its loss correlates with poor prognosis in cancers like leukemia and breast cancer. Commercial CABIN1 antibodies are typically raised against specific epitopes, such as the N-terminal (1-300 aa) or C-terminal regions, with validation in knockout models to ensure specificity. Ongoing studies aim to clarify CABIN1's dual roles as a context-dependent oncogene or tumor suppressor, highlighting its therapeutic potential in targeting calcineurin-related pathologies.