Recombinant Human Transferrin Receptor protein (GST tag N-Terminus)
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Recombinant Human Transferrin Receptor protein (GST tag N-Terminus) is a Human Fragment protein, in the 68 to 168 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
CD71, Transferrin receptor protein 1, TR, TfR, TfR1, Trfr, T9, Transferrin receptor 1, p90, TFRC
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Transferrin Receptor protein (GST tag N-Terminus) (AB159687)
ab159687 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
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.
Pathways
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.
Specifications
Form
Liquid
General info
Function
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.. (Microbial infection) Acts as a host entry factor for rabies virus that hijacks the endocytosis of TFRC to enter cells.. (Microbial infection) Acts as a host entry factor for SARS-CoV, MERS-CoV and SARS-CoV-2 viruses that hijack the endocytosis of TFRC to enter cells.. (Microbial infection) Acts as a receptor for Plasmodium vivax.
Sequence similarities
Belongs to the peptidase M28 family. M28B subfamily.
Post-translational modifications
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).. N- and O-glycosylated, phosphorylated and palmitoylated. The serum form is only glycosylated.. Proteolytically cleaved on Arg-100 to produce the soluble serum form (sTfR).. Palmitoylated on both Cys-62 and Cys-67. Cys-62 seems to be the major site of palmitoylation.
Target data
Product promise
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