Overview
- Peptide (C)EDEFRYRMYQTQVSD, corresponding to amino acid residues 635 - 649 of mouse PTGFRN (Accession Q9WV91). Extracellular, N-terminus.
PTGFRN (extracellular) Blocking Peptide (#BLP-NR212)
The Prostaglandin F2 Receptor Negative Regulator (PTGFRN), also known as EWI-F and CD9P-1, is a member of the immunoglobulin (Ig) superfamily. PTGFRN is a type I single-pass transmembrane protein and part of the cell adhesion molecule (CAM) family, which plays essential roles in cell-cell and cell-matrix interactions1,2.
CAMs, including PTGFRN, are characterized by extracellular Ig-like domains and contribute to cellular adhesion, migration, and signaling. PTGFRN interacts with tetraspanins (CD9, CD81), integrins, and ERM proteins, functioning as a scaffold in tetraspanin-enriched microdomains (TEMs)3. These interactions enable its role in tumor progression, metastasis, and angiogenesis by regulating PI3K/AKT and mTOR signaling pathways1,2.
PTGFRN is highly expressed in glioblastoma (GBM) and several cancers, with significantly elevated levels in tumor tissues compared to normal tissues1,2,3. It is implicated in tumor proliferation, migration, and radiation resistance. In neurodegenerative disorders, PTGFRN correlates with Alzheimer’s disease progression via its role in extracellular vesicles (EVs) associated with amyloid plaques3.
PTGFRN’s association with poor prognosis in cancers and its involvement in neurodegeneration highlight its potential as a therapeutic target. Immunodetection of PTGFRN can benefit research areas in oncology, neurobiology, and regenerative medicine1,2,4.