The Recombinant Mouse Transferrin/TF Protein is a high-quality recombinant protein designed for murine biological research applications. This protein serves as an essential reagent in mouse model studies, comparative immunology research, and preclinical therapeutic evaluations, enabling scientists to investigate Transferrin/TF biology and its relevance to human disease mechanisms through translational research approaches.
This product (SKU: RPCB1667) is produced using HEK293 cells and features a C-hFc tag for convenient detection and purification. The protein exhibits a calculated molecular weight of 100.85 kDa with an observed molecular weight of 100-120 kDa under denaturing conditions, achieving ≥ 95 % as determined by SDS-PAGE.. Functional bioactivity has been validated through rigorous quality control assays, confirming its suitability for demanding research applications.
High quality, high purity and low endotoxin recombinant Recombinant Mouse Transferrin/TF Protein (RPCB1667), tested reactivity in HEK293 cells and has been validated in SDS-PAGE.100% guaranteed.
Endotoxin:
< 0.1 EU/μg of the protein by LAL method.
Purity:
≥ 95 % as determined by SDS-PAGE.
Formulation:
Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.
Bio-Activity:
Measured by its binding ability in a functional ELISA.Immobilized Mouse sTfR/CD71 (RPCB1443) at 5 μg/mL (100 μL/well) can bind Mouse Transferrin/TF (RPCB1667) with a linear range of 0.002-1.8 ng/mL.
Reconstitution:
Centrifuge the vial before opening. Reconstitute to a concentration of 0.1-0.5 mg/mL in sterile distilled water. Avoid vortex or vigorously pipetting the protein. For long term storage, it is recommended to add a carrier protein or stablizer (e.g. 0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose), and aliquot the reconstituted protein solution to minimize free-thaw cycles.
Storage:
Store at -20℃.Store the lyophilized protein at -20℃ to -80 ℃ up to 1 year from the date of receipt. After reconstitution, the protein solution is stable at -20℃ for 3 months, at 2-8℃ for up to 1 week.
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.
Recombinant Mouse Transferrin/TF Protein was determined by SDS-PAGE under reducing conditions with Coomassie Blue.
Immobilized Mouse sTfR/CD71 (RPCB1443) at 5 μg/mL (100 μL/well) can bind Mouse Transferrin/TF (RPCB1667) with a linear range of 0.002-1.8 ng/mL.
