TFRC Protein, Human (Biotinylated, HEK293, His-Avi)

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 (Biotinylated, HEK293, His-Avi) is the recombinant human-derived TFRC protein, expressed by HEK293 , with C-Avi, N-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, His-Avi Tag at 2 μg/mL (100 μL/well) on the plate. Dose response curve for Biotinylated Human Transferrin R, His Tag with the EC₅₀ of 60-70 ng/mL determined by ELISA.

Human

HEK293

N-Avi;N-6*His

P02786 (C89-F760)

7037  [NCBI]

Extracellular Domain

Biotin

The single lysine residue in Avitag is biotinylated through an enzymatic reaction.

CKGVEPKTECERLAGTESPVREEPGEDFPAARRLYWDDLKRKLSEKLDSTDFTGTIKLLNENSYVPREAGSQKDENLALYVENQFREFKLSKVWRDQHFVKIQVKDSAQNSVIIVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTKKDFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHTQFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTDSTCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEPDHYVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDMVLKDGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFTYINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQFLYQDSNWASKVEKLTLDNAAFPFLAYSGIPAVSFCFCEDTDYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIKLTHDVELNLDYERYNSQLLSFVRDLNQYRADIKEMGLSLQWLYSARGDFFRATSRLTTDFGNAEKTDRFVMKKLNDRVMRVEYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRKQNNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNEF

Approximately 78-100 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

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

Lyophilized powder.

1.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4. Normally 8% trehalose is added as protectant before lyophilization.
2.Lyophilized from a 0.22 μm filtered solution of PBS, 200 mM L-arginine, 8% trehalose, pH 7.4.
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.

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.