Soluble Human Transferrin Receptor (sTFR, TFR1)

This soluble portion of the human transferrin receptor (sTFR, residues 121 - 760) is expressed in BHK cells (eukaryotic), has a hexa His tag, a Factor Xa cleavage site, and three glycosylation sites at positions Asn251, Asn317 and Asn727. Also known as (Cluster of Differentiation 71) (CD71), or p90,  sTfR is a protein that in humans is encoded by the TFRC gene.

Transferrins are bilobal iron-binding glycoproteins that are responsible for tightly binding two atoms of iron acquired from the diet for transport through blood and delivery to cells. Iron-saturated transferrin binds to transferrin receptors on the cell surface, and the complex is internalized by receptor-mediated endocytosis. The transferrin receptor system is one of the most well characterized pathways for cell uptake and recombinant forms of transferrin have been used to deliver short peptides and toxins into cells. Furthermore the transferrin receptor is targeted by a number of "New World" viruses during early steps of infection (eg. Machupo virus).

From the laboratory of Anne B. Mason, PhD, University of Vermont.

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Catalog Number Product Size AVAILABILITY Price Qty
EVM001
Soluble Human Transferrin Receptor (sTFR, TFR1), 50ug
50ug Unavailable
Price: $161.00
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Specifications
Product Type: Protein
Name: For purchase, soluble portion of the human transferrin receptor (sTFR)
Source: Expressed in Baby hamster kidney (BHK) cells. Produced as a secreted protein from the BHK cells into the tissue culture medium.
Molecular Weight: The calculated mass of the sTFR (residues 121-760) is 71726 Da to which is added 440 Da for the VPDK sequence, 823 Da for the hexa-His tag, and 456 Da for the factor Xa cleavage sequence for a total mass of 73445 Da. The mass spec analysis indicates a mass of 79700 Da The difference is attributed to the three glycans
Amino Acid Sequence: VPDKHHHHHHIEGRRLYWDDLKRKLSEKLDSTDFTGTIKLLNENSYVPREAGSQKDENLALYVENQFREFKLSKVWRDQHFVKIQVKDSAQNSVIIVDKNGRLVYLVENPGGYVAYSKAATVTGKLVHANFGTKKDFEDLYTPVNGSIVIVRAGKITFAEKVANAESLNAIGVLIYMDQTKFPIVNAELSFFGHAHLGTGDPYTPGFPSFNHTQFPPSRSSGLPNIPVQTISRAAAEKLFGNMEGDCPSDWKTDSTCRMVTSESKNVKLTVSNVLKEIKILNIFGVIKGFVEPDHYVVVGAQRDAWGPGAAKSGVGTALLLKLAQMFSDMVLKDGFQPSRSIIFASWSAGDFGSVGATEWLEGYLSSLHLKAFTYINLDKAVLGTSNFKVSASPLLYTLIEKTMQNVKHPVTGQFLYQDSNWASKVEKLTLDNAAFPFLAYSGIPAVSFCFCEDTDYPYLGTTMDTYKELIERIPELNKVARAAAEVAGQFVIKLTHDVELNLDYERYNSQLLSFVRDLNQYRADIKEMGLSLQWLYSARGDFFRATSRLTTDFFGNAEKTDRFVMKKLNDRVMRVEYHFLSPYVSPKESPFRHVFWGSGSHTLPALLENLKLRKQNNGAFNETLFRNQLALATWTIQGAANALSGDVWDIDNEF
Fusion Tag(s): Hexa His tag on amino terminus
Purity: >95% pure. Used to obtain crystal structure (see Eckenroth BE et al. PNAS. 2011)
Buffer: Soluble portion of transferrin receptor protein which is a homodimer in solution of 100 mM ammonium bicarbonate
Concentration: ~1mg/mL, Soluble at concentrations of 1-2mg/mL and possibly higher at neutral pH. Aggregates at lower pH values
Storage: Store at 4 C. Do not freeze.
Shipped: Cold packs
Data

SDS-PAGE Analysis

 Lane 1, MW ladder; Lane 2, purified sTFR.

Provider
From the laboratory of Anne B. Mason, PhD, University of Vermont.
References
  1. Byrne, S. L., R. Leverence, J.S. Klein, A.M. Giannetti, V.C. Smith, R.T.A. MacGillivray, I.A. Kaltashov, and A.B. Mason, ‘Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptor’, Biochemistry 45, 6663-6673 (2006).
  2. Byrne, S.L., N. D. Chasteen, A. N. Steere and A.B. Mason, 'The unique kinetics of iron release from transferrin: The role of receptor, lobe-lobe interactions, and salt at endosomal pH ‘.J. Mol Biol 396, 130-140 (2010).
  3. Eckenroth, B.E., A.N. Steere, N. Dennis Chasteen and S. J. Everse, and A.B. Mason, 'How the binding of human transferrin primes the transferrin receptor potentiating iron release at endosomal pH', Proc. Natl. Acad. Sci, USA, 108, 13089-13094 (2011)
  4. Steere, A.N., B.F. Miller, S.E. Roberts, S.L. Byrne, N. D. Chasteen, V.C. Smith, R.T.A. MacGillivray and A.B. Mason, 'Ionic residues of human serum transferrin affect binding to the transferrin receptor and iron release', Biochemistry, 51, 686-694 (2012).
  5. Cox HD, Miller GD, Lai A, Cushman D, Eichner D. Detection of autologous blood transfusions using a novel dried blood spot method. Drug Test Anal. 2017 Nov;9(11-12):1713-1720. View Article

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