Transferrin (mouse, recombinant)

Serotransferrin|Siderophilin|β-1 Metal-binding Globulin

Transferrin is a glycoprotein that binds and transports ferric iron.{46988,46990} It is a bilobal protein composed of N- and C-terminal lobes, each housing a ferric iron binding site, connected by a seven-amino acid bridge.{46988} Transferrin is predominately synthesized in hepatocytes, but is also expressed in Sertoli, ependymal, oligodendroglial, and metastatic melanoma cell lines, and is secreted into the circulation.{46988,46990} Iron-containing transferrin binds to the transferrin receptor (TFR1; Item No. 32031) on the surface of iron-requiring cells to form the transferrin/TFR complex which undergoes clathrin-dependent endocytosis to facilitate intracellular iron release. The transferrin/TFR complex is then returned to the cell surface and apo-transferrin is released back into the circulation via dissociation or displacement by an iron-containing transferrin.{46988} Immunodepletion of transferrin inhibits serum-induced ferroptosis of Bax and Bak double knockout mouse embryonic fibroblasts (MEFs), indicating that transferrin is a regulator of ferroptosis.{43380} Exogenous administration of apo-transferrin to three-day-old rats increases expression of myelin constituents and enhances myelinogenesis in myelin-deficient rats.{46991} It also normalizes labile plasma iron concentrations and red blood cell survival, increases hemoglobin production, and decreases reticulocytosis and splenomegaly in the Hbbth1/th1 mouse model of β-thalassemia.{46989} Cayman’s Transferrin (mouse, recombinant) protein can be used for cell-based assays. This protein consists of 689 amino acids, has a calculated molecular weight of 76.3 kDa, and a predicted N-terminus of Val20 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 61-66 kDa due to glycosylation.

-80

-80

Lyophilized from sterile PBS, pH 7.4

365

≥95% estimated by SDS-PAGE