The protein tyrosine phosphatase non-receptor type 13 (PTPN13), also known as PTP-BAS or PTP1E, is a cytoplasmic enzyme encoded by the PTPN13 gene. It belongs to the protein tyrosine phosphatase (PTP) family, which regulates cellular signaling by dephosphorylating tyrosine residues on target proteins. PTPN13 contains multiple functional domains, including a FERM domain for membrane association and PDZ domains for protein-protein interactions, enabling its role in diverse signaling pathways. It interacts with key regulators of apoptosis (e.g., Fas receptor), growth (e.g., EGFR), and cytoskeletal organization.
PTPN13 is implicated in cancer progression, acting as a tumor suppressor or promoter depending on context. Reduced PTPN13 expression correlates with poor prognosis in breast, colon, and lung cancers, while hyperactivation links to drug resistance in melanoma. Its dual roles stem from interactions with oncogenic or apoptotic pathways. Additionally, PTPN13 mutations or altered expression are observed in autoimmune diseases and neurological disorders.
Antibodies targeting PTPN13 are vital tools for studying its expression, localization, and post-translational modifications. They are used in techniques like Western blotting, immunohistochemistry, and co-immunoprecipitation to explore its regulatory mechanisms. However, challenges remain in understanding isoform-specific functions and context-dependent signaling effects. Research on PTPN13 antibodies may advance therapeutic strategies for cancers and immune-related diseases by modulating phosphatase activity or associated pathways.