The Epithelial Splicing Regulatory Protein 1 (ESRP1) is an RNA-binding protein critical for regulating alternative splicing events in epithelial cells. It governs the production of splice variants that maintain epithelial phenotypes by modulating cell adhesion, polarity, and signaling. ESRP1 is particularly notable for its role in the epithelial-mesenchymal transition (EMT), a process central to development, wound healing, and cancer metastasis. During EMT, ESRP1 expression is downregulated, promoting a shift to mesenchymal splicing patterns that enhance cell motility and invasiveness.
ESRP1 antibodies are essential tools for studying its expression, localization, and functional roles. They are widely used in techniques like Western blotting, immunofluorescence, and immunohistochemistry to assess ESRP1 levels in tissues or cell lines, particularly in cancer research. Reduced ESRP1 expression correlates with poor prognosis in carcinomas, making it a potential biomarker for metastatic potential. Additionally, these antibodies aid in exploring ESRP1's interaction with RNA targets and its regulatory crosstalk with signaling pathways (e.g., FGFR2 or CD44 splicing).
Research on ESRP1 antibodies also supports therapeutic investigations, as restoring ESRP1 activity might counteract pro-metastatic splicing programs. However, challenges remain in standardizing antibody specificity across experimental models. Overall, ESRP1 antibodies are pivotal for unraveling post-transcriptional mechanisms in epithelial biology and disease.