Recombinant Mouse FOLR2 Protein, CF Summary
Met-Ser227, with a C-terminal 6-His tag
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Folate Receptor 2 (FOLR2), also known as Folate Receptor beta, is a 38 kDa protein that mediates the cellular uptake of folic acid and reduced folates. Dietary folates are required for many key metabolic processes including nucleotide and methionine synthesis, the interconversion of glycine and serine, and histidine breakdown (1, 2). Mature FOLR2 is an N-glycosylated protein that is anchored to the cell surface by a GPI linkage (3 - 5). Mouse FOLR2 shares 82% and 91% amino acid sequence identity with human and rat FOLR2, respectively. FOLR2 is predominantly expressed in placenta, cells of the neutrophilic lineage, and some CD34+ hematopoietic progenitor cells (4, 6, 7). It is up‑regulated on myeloid leukemias, head and neck squamous cell carcinomas, and several nonepithelial cancers (3, 6, 8). It is also up‑regulated on immunosuppressive tumor-associated macrophages as well as on macrophages and monocytes at chronic inflammatory sites including rheumatoid arthritis synovium and glioblastoma (9 - 12). FOLR2 knockout mice do not show gross morphological defects, but they exhibit increased sensitivity to arsenate-induced teratogenicity (13, 14).
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