This product is an unconjugated, non-therapeutic recombinant analog of the anti-FOLR1 antibody mirvetuximab, supplied for research use only and not for human or veterinary use. It is a full-length human IgG1-kappa built around the folate receptor alpha (FOLR1/FRalpha) target, carrying the E356D/M358L allotype substitutions in the Fc region. As an unconjugated analog it reproduces the antigen-binding specificity of the originator without the maytansinoid payload (DM4) of the clinical antibody-drug conjugate, making it well suited to controlled comparisons. Researchers use it as a positive binding control, as a benchmarking reagent for FOLR1-directed assay development, and as the antibody backbone for in-house ADC or conjugation chemistry. It supports flow cytometry, ELISA, immunoprecipitation, and cell-based binding/blocking studies, and serves as an isotype-matched reference in preclinical FOLR1-targeting programs. The material is offered at research-grade low endotoxin (<1 EU/mg), with ultra-low endotoxin (<0.5 EU/mg) and bulk mg-to-gram quantities available for scale-up and in-vitro standardization.
Folate receptor alpha (FOLR1, FRalpha; UniProt P15328) is a glycosylphosphatidylinositol (GPI)-anchored cell-surface glycoprotein that binds folate (vitamin B9) with high affinity and mediates its cellular uptake via receptor-mediated endocytosis, complementing the reduced folate carrier. Folate delivered through this pathway supports one-carbon metabolism, nucleotide synthesis, and methylation reactions essential for proliferating cells. FOLR1 expression is restricted in normal tissues, largely to the apical surface of certain epithelia (kidney, lung, choroid plexus), but is markedly overexpressed in many epithelial cancers, notably ovarian, endometrial, and non-small-cell lung carcinomas. This tumor-associated overexpression and limited accessibility in normal tissue make FOLR1 an attractive antigen for targeted therapeutics, imaging agents, and antibody-drug conjugates. Its GPI anchor and apical localization influence antibody accessibility and internalization kinetics, both relevant to conjugate and neutralization studies.