Transferrin Protein (His Tag) (recombinant human)

Activity: Measured by its binding ability in a functional ELISA. Immobilized human CD71 at 10 µg/ml (100 µl/well) can bind human Transferrin. The EC50 of human Transferrin is 5.6 ng/mL.2. Measured in a serum-free cell proliferation assay using MCF-7 human breast cancer cells. Karey, K.P. et al. (1988) Cancer Research 48:4083. The ED50 for this effect is typically 0.01-0.04 µg/mL. Protein Construction: A DNA sequence encoding the human transferrin (NP_001054.1) (Met 1-Pro 698) was fused with a polyhistidine tag at the C-terminus. Sequence: Met 1-Pro 698. Fusion tag: C-His Endotoxin: < 1.0 EU per µg of the protein as determined by the LAL method. Apparent Molecular Mass: 74 kDa. Protein function: Transferrin is a glycoprotein with an approximate molecular weight of 76.5 kDa. This glycoprotein is thought to have been created as a result of an ancient gene duplication event that led to generation of homologous C and N-terminal domains each of which binds one ion of ferric iron. The function of Transferrin is to transport iron from the intestine, reticuloendothelial system, and liver parenchymal cells to all proliferating cells in the body. This protein may also have a physiologic role as granulocyte / pollen-binding protein (GPBP) involved in the removal of certain organic matter and allergens from serum. Transferrins are iron binding transport proteins which bind Fe3+ ion in association with the binding of an anion, usually bicarbonate. This transferrin binds only one Fe3+ ion per protein molecule. Transports iron ions from the hemolymph into the eggs during the vitellogenic stage. Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an ani Protein function: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. [The UniProt Consortium]