Recombinant Human Transferrin Receptor protein (denatured) is a Human Fragment protein, in the 89 to 760 aa range, expressed in Escherichia coli, with >80% purity and suitable for SDS-PAGE.
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes (PubMed:26214738). 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 (By similarity). A second ligand, the hereditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. Positively regulates T and B cell proliferation through iron uptake (PubMed:26642240). Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway (PubMed:26214738). When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion (PubMed:26214738). When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2 (PubMed:26214738). Mediates uptake of NICOL1 into fibroblasts where it may regulate extracellular matrix production (By similarity). (Microbial infection) Acts as a receptor for new-world arenaviruses: Guanarito, Junin and Machupo virus.
CD71, Transferrin receptor protein 1, TR, TfR, TfR1, Trfr, T9, p90, TFRC
Recombinant Human Transferrin Receptor protein (denatured) is a Human Fragment protein, in the 89 to 760 aa range, expressed in Escherichia coli, with >80% purity and suitable for SDS-PAGE.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.32% Tris HCl
ab202198 was purified by conventional chromatography techniques.
Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes (PubMed:26214738). 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 (By similarity). A second ligand, the hereditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. Positively regulates T and B cell proliferation through iron uptake (PubMed:26642240). Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway (PubMed:26214738). When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion (PubMed:26214738). When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2 (PubMed:26214738). Mediates uptake of NICOL1 into fibroblasts where it may regulate extracellular matrix production (By similarity).
Belongs to the peptidase M28 family. M28B subfamily.
Stearoylated by ZDHHC6 which inhibits TFRC-mediated activation of the JNK pathway and promotes mitochondrial fragmentation (PubMed:26214738). Stearoylation does not affect iron uptake (PubMed:26214738).
The transferrin receptor commonly referred to as TfR or CD71 is an integral membrane protein that facilitates the uptake of transferrin-bound iron into cells. This receptor has a molecular weight of around 95 kDa and often exists as a homodimer on the cell surface. It is widely expressed in many tissues especially in erythroid precursors and rapidly dividing cells. Alternate names for this receptor include TfR1 and TfR2 though they have distinct roles and distributions. Other transmembrane proteins like OX26 and MEM have been studied in relation to the transferrin receptor due to their involvement in drug delivery.
TfR plays a critical role in iron homeostasis by mediating the internalization of transferrin and release of iron in the endosomes. It operates as part of the transferrin-transferrin receptor complex facilitating iron assimilation necessary for DNA synthesis and cell growth. Iron release involves acidifying endosomes allowing transferrin to bind with specific cellular receptors including alternate forms like beta 2 transferrin. The process subsequently contributes to erythropoiesis and various metabolic processes by regulating essential cellular iron levels.
The transferrin receptor is central to iron metabolism and the receptor-mediated endocytosis pathway. It tightly interacts with transferrin and intracellular pathways process the iron released from transferrin within endosomes. The receptor's role in this pathway involves a dynamic with other proteins such as HFE and hepcidin. These interactions help control systemic iron levels linking closely to the maintenance of erythroid cell health and proliferation.
Disruptions in transferrin receptor function correlate with anemia and neurodegenerative disorders. In anemia related to iron deficiency impaired TfR activity reduces iron uptake culminating in insufficient erythropoiesis. Altered receptor expression or function also connects to neurological diseases like Alzheimer's where iron dysregulation is a concern. Here the transferrin receptor interacts with proteins like Amyloid precursor protein contributing to disease pathology through improper metal homeostasis.
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15% SDS-PAGE analysis of ab202198 (3ug).
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