FOLR1 is a glycosylphosphatidylinositol (GPI)-anchored protein that facilitates unidirectional folate transport into cells, critical for DNA synthesis and methylation . Its overexpression in ovarian, lung, and breast cancers makes it a prime target for monoclonal antibody (mAb) development. FOLR1 antibodies are engineered to bind specifically to this receptor, enabling:
Therapeutic interventions via antibody-dependent cellular cytotoxicity (ADCC) or complement activation .
Key advancements in FOLR1 antibody development include:
Immunogen Design: Full-length FOLR1 protein was used to generate mAbs targeting non-overlapping epitopes, ensuring robust detection across diagnostic platforms .
Specificity Validation: Antibodies like MAB5646 (R&D Systems) show no cross-reactivity with FOLR2, FOLR3, or FOLR4 .
FOLR1 antibodies exert effects through:
ADCC: Farletuzumab binds FOLR1 on cancer cells, recruiting natural killer (NK) cells via Fcγ receptors (e.g., CD16a) to induce tumor lysis .
Diagnostic Binding: MAB5646 detects FOLR1 at ~40 kDa in Western blots and shows membrane localization in flow cytometry .
FOLR1 antibodies are critical for:
Tissue Staining: Immunohistochemistry identifies FOLR1 overexpression in ovarian cancer biopsies .
Flow Cytometry: MCF-7 breast cancer cells show strong FOLR1 surface expression when stained with MAB5646 .
Preclinical Studies: Farletuzumab reduced tumor growth in xenograft models by 60–70% via ADCC .
Clinical Trials: Phase II trials demonstrated safety and efficacy in platinum-sensitive ovarian cancer .