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Folate Receptor 1 (FOLR1), also known as Folate Receptor alpha (FRα) or Folate Binding Protein (FBP), is a high-affinity receptor for folic acid and its reduced derivatives. It plays a crucial role in the cellular uptake of folates, which are essential for various metabolic processes, including nucleotide synthesis, methionine synthesis, and the interconversion of glycine and serine .
FOLR1 is a glycoprotein that can exist in two forms: membrane-bound and soluble. The membrane-bound form is anchored to the cell surface via a glycosyl-phosphatidylinositol (GPI) linkage, while the soluble form can be found in bodily fluids such as serum and breast milk . The receptor is predominantly expressed on epithelial cells and is significantly upregulated in various carcinomas, including breast and ovarian cancers .
FOLR1 is essential for embryonic development and normal cell proliferation. It facilitates the transfer of 5-methyltetrahydrofolate and other folate analogs into cells, supporting critical metabolic pathways . Mutations in the FOLR1 gene have been associated with neurodegenerative conditions due to cerebral folate transport deficiency .
Recombinant human FOLR1 is produced using various expression systems, including HEK293 and CHO cells. The recombinant protein is typically tagged with a polyhistidine (His) tag to facilitate purification and detection . The recombinant form retains the functional properties of the native protein, making it valuable for research and therapeutic applications.
Recombinant FOLR1 is used in various research applications, including: