Transferrin Recombinant Protein

Transferrin Protein, Human, Recombinant, HPLC-verified

Cat. Num. AAA259181

• Purity: >= 95% as determined by SDS-PAGE.; = 95% as determined by SEC-HPLC.
• Synonyms: Transferrin; N/A; Transferrin Protein, Human, Recombinant, HPLC-verified; transferrin; HEL-S-71p Protein, Human; PRO1557 Protein, Human; PRO2086 Protein, Human; TFQTL1 Protein, Human; Transferrin Protein, Human; Transferrin recombinant protein

• Host: HEK293 Cells
• Purity/Purification: >= 95% as determined by SDS-PAGE.; = 95% as determined by SEC-HPLC.
• Form/Format: Lyophilized from sterile PBS, pH 7.4.; Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.

• Species: Human
• Predicted N Terminal: Val 20
• Endotoxin: <1.0 EU per ug protein as determined by the LAL method.
• Protein Construction: A DNA sequence encoding the Human TF (NP_001054.2)(Val20-Pro698) was expressed.
• Activity: Immobilized Recombinant Human Transferrin protein at 2 ug/mL (100 uL/well) can bind Recombinant Human Transferrin Receptor/TFRC Protein(His Tag),Biotinylated , the EC50 is 30-90 ng/mL.
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Application Data

(Immobilized Recombinant Human Transferrin protein (#AAA259181) at 2 ug/mL (100 uL/well) can bind Recombinant Human Transferrin Receptor/TFRC Protein(His Tag),Biotinylated (Cat: 11020-H07H-B), the EC50 is 30-90 ng/mL.)

Application Data

Application Data

Related Product Information for Transferrin recombinant protein

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 that 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 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. When a transferrin loaded with iron encounters with a transferring receptor on cell surface, transferring binds to it and, as a consequence, is transported into the cell in a visicle by receptor-mediated endocytosis. The PH is reduced by hydrogen iron pumps. The lower pH causes transferrin to release its iron ions. The receptor is then transported through the endocytic cycle back to the cell surface, ready for another round of iron uptake. Each transferrin molecule has the ability to carry two iron ions in the ferric form.

References

Ponka P, et al. (1998) Function and regulation of transferrin and ferritin. Semin Hematol. 35(1): 35-54.
Wagner E, et al. (1990) Transferrin-polycation conjugates as carriers for DNA uptake into cells. Proc Natl Acad Sci. 87(9): 3410-4.Cheng Y, et al. (2004) Structure of the human transferrin receptor-transferrin complex. Cell. 116 (4): 565-76.

NCBI and Uniprot Product Information

• Molecular Weight: The recombinant Human TF consists of 679 amino acids and predicts a molecular mass of 75.19 kDa. It migrates as an approximately 79.4 kDa band in SDS-PAGE under reducing conditions.