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Transferrin Receptor/TFRC Protein, Human, Recombinant (aa 101-760, His)

Catalog No. TMPJ-00378

Transferrin receptor protein 1 (TFRC) belongs to the peptidase M28 family that is synthesized as a 172 amino acid (aa). TFRC regulated by cellular iron levels through binding of the iron regulatory proteins, IRP1 and IRP2, to iron-responsive elements in the 3'-UTR. It binds one transferrin or HFE molecule per subunit and binds the HLA class II histocompatibility antigen, DR1. It Interacts with SH3BP3 and STEAP3, facilitates TFRC endocytosis in erythroid precursor cells. Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system. A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. It positively regulates T and B cell proliferation through iron uptake.

Transferrin Receptor/TFRC Protein, Human, Recombinant (aa 101-760, His)

Transferrin Receptor/TFRC Protein, Human, Recombinant (aa 101-760, His)

Catalog No. TMPJ-00378
Transferrin receptor protein 1 (TFRC) belongs to the peptidase M28 family that is synthesized as a 172 amino acid (aa). TFRC regulated by cellular iron levels through binding of the iron regulatory proteins, IRP1 and IRP2, to iron-responsive elements in the 3'-UTR. It binds one transferrin or HFE molecule per subunit and binds the HLA class II histocompatibility antigen, DR1. It Interacts with SH3BP3 and STEAP3, facilitates TFRC endocytosis in erythroid precursor cells. Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system. A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. It positively regulates T and B cell proliferation through iron uptake.
Pack SizePriceAvailabilityQuantity
10 μg$977-10 days
50 μg$2727-10 days
500 μg$1,3707-10 days
1 mg$1,9807-10 days
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Product Information

Biological Activity
Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description
Transferrin receptor protein 1 (TFRC) belongs to the peptidase M28 family that is synthesized as a 172 amino acid (aa). TFRC regulated by cellular iron levels through binding of the iron regulatory proteins, IRP1 and IRP2, to iron-responsive elements in the 3'-UTR. It binds one transferrin or HFE molecule per subunit and binds the HLA class II histocompatibility antigen, DR1. It Interacts with SH3BP3 and STEAP3, facilitates TFRC endocytosis in erythroid precursor cells. Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system. A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. It positively regulates T and B cell proliferation through iron uptake.
Species
Human
Expression System
HEK293 Cells
TagN-6xHis
Accession NumberP02786
Synonyms
Trfr,Transferrin receptor protein 1,TR,TfR,T9,p90
Amino Acid
Leu101-Phe760
Construction
Leu101-Phe760
Protein Purity
Greater than 95% as determined by reducing SDS-PAGE. Greater than 95% as determined by SEC-HPLC.
Molecular Weight80-90 KDa (reducing condition)
Endotoxin< 0.1 ng/µg (1 EU/µg) as determined by LAL test.
FormulationLyophilized from a solution filtered through a 0.22 μm filter, containing 20 mM PB, 150 mM NaCl, 5% Trehalose, 5% Mannitol, 0.01% Tween 80, pH7.4.
Reconstitution
Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.
Stability & Storage
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
ShippingIn general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
Research Background
Transferrin receptor protein 1 (TFRC) belongs to the peptidase M28 family that is synthesized as a 172 amino acid (aa). TFRC regulated by cellular iron levels through binding of the iron regulatory proteins, IRP1 and IRP2, to iron-responsive elements in the 3'-UTR. It binds one transferrin or HFE molecule per subunit and binds the HLA class II histocompatibility antigen, DR1. It Interacts with SH3BP3 and STEAP3, facilitates TFRC endocytosis in erythroid precursor cells. Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system. A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. It positively regulates T and B cell proliferation through iron uptake.

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