TFRC Protein, Human (HEK293, His)

TFRC protein promotes cellular iron uptake through receptor-mediated endocytosis. TFRC is essential for erythroid and nervous system development and plays a crucial role in iron homeostasis. TFRC Protein, Human (HEK293, His) is the recombinant human-derived TFRC protein, expressed by HEK293 , with N-6*His labeled tag.

TFRC protein facilitates cellular iron uptake through receptor-mediated endocytosis of ligand-occupied transferrin receptors into specialized endosomes, as documented in studies. This process involves endosomal acidification, leading to iron release, followed by recycling of the apotransferrin-receptor complex to the cell surface, accompanied by a return to neutral pH and the subsequent loss of apotransferrin affinity for its receptor. Crucial for erythrocyte and nervous system development, TFRC is a vital player in iron homeostasis. The hereditary hemochromatosis protein HFE competes with transferrin for binding at an overlapping C-terminal site. TFRC positively regulates T and B cell proliferation through iron uptake and acts as a lipid sensor, modulating mitochondrial fusion by regulating the JNK pathway. Depending on dietary stearate levels, TFRC either promotes JNK pathway activation and degradation of the mitofusin MFN2 when stearate is low or inhibits JNK pathway activation and MFN2 degradation when stearate is high. Furthermore, TFRC acts as a receptor for new-world arenaviruses, including Guanarito, Junin, and Machupo virus, during microbial infection.

Immobilized Human Transferrin at 2 μg/mL (100 μL/well) can bind Biotinylated Human Transferrin R that produces 50% of the optimal binding response is found to be approximately <59 ng/mL.

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  Immobilized Human Transferrin at 2 μg/mL (100 μL/well) can bind Biotinylated Human Transferrin R The ED₅₀ for this effect is 6.822 ng/mL.

Human

HEK293

N-6*His

P02786 (L101-F760)

7037  [NCBI]

Partial

LAGTESPVREEPGEDFPAARRLYWDDLKRKLSEKLDSTDFTGTIKLLNENSYVPREAGSQKDENLALYVENQFREFKLSKVWRDQHFVKIQVKDSAQNSVIIVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTKKDFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHTQFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTDSTCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEPDHYVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDMVLKDGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFTYINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQFLYQDSNWASKVEKLTLDNAAFPFLAYSGIPAVSFCFCEDTDYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIKLTHDVELNLDYERYNSQLLSFVRDLNQYRADIKEMGLSLQWLYSARGDFFRATSRLTTDFGNAEKTDRFVMKKLNDRVMRVEYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRKQNNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNEF

Approximately 75-90 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

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  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder

1.Lyophilized from a 0.22 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.4.
2.Lyophilized from a 0.22 μm filtered solution of 20 mM PB, 150 mM NaCl, 5% trehalose, 5% mannitol, 0.01% Tween 80, pH7.4.
3.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% trehalose.
Please refer to the lot-specific COA for specific buffer information.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.