Active • Host: HEK293 cells • AA: 20-698 • Tag: C-terminal His • MW: 76.6 kDa
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Transferrin (human, recombinant)

Item No. 32030

Technical Information
Synonyms
  • HEL-S-71p
  • β-1 Metal-binding Globulin
  • TFQTL1
  • Serotransferrin
  • Siderophillin
Purity
≥95% estimated by SDS-PAGE
Endotoxin Testing
<1.0 EU/μg, determined by the LAL endotoxin assay
Source
Active recombinant human C-terminal His-tagged transferrin expressed in HEK293 cells
Amino Acids
20-698
MW
76.6 kDa
Lyophilized from sterile PBS, pH 7.4
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    Transferrin is a glycoprotein that binds and transports ferric iron.1,2 It is a 679-amino acid bilobal protein composed of N- and C-terminal lobes, each housing a ferric iron binding site, connected by a seven-amino acid bridge.1 Transferrin is predominately synthesized in hepatocytes, but is also expressed in Sertoli, ependymal, oligodendroglial, and metastatic melanoma cell lines, and is secreted into the circulation.1,2 Iron-containing transferrin binds to the transferrin receptor (TfR1; Item No. 32031) on the surface of iron-requiring cells to form the transferrin/TfR complex, which undergoes clathrin-dependent endocytosis to facilitate intracellular iron release. The transferrin/TfR complex is then returned to the cell surface and apo-transferrin is released back into the circulation via dissociation or displacement by an iron-containing transferrin.1 Immunodepletion of transferrin inhibits serum-induced ferroptosis of Bax and Bak double knockout mouse embryonic fibroblasts (MEFs), indicating that transferrin is a regulator of ferroptosis.3 Exogenous administration of apo-transferrin to three-day-old rats increases expression of myelin constituents and enhances myelinogenesis in myelin-deficient rats.4 It also normalizes labile plasma iron concentrations and red blood cell survival, increases hemoglobin production, and decreases reticulocytosis and splenomegaly in the Hbbth1/th1 mouse model of β-thalassemia.5 Cayman’s Transferrin (human, recombinant) protein can be used for ELISA and cell-based assay applications. This protein consists of 690 amino acids, has a calculated molecular weight of 76.6 kDa, and a predicted N-terminus of Val20 after signal peptide cleavage.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Luck, A.N., and Mason, A.B. Transferrin-mediated cellular iron delivery. Curr. Top. Membr. 69, 3-35 (2012).

    2. Gomme, P.T., and McCann, K.B. Transferrin: Structure, function and potential therapeutic actions. Drug Discov. Today 10(4), 267-273 (2005).

    3. Gao, M., Monian, P., Quadri, N., et alGlutaminolysis and transferrin regulate ferroptosis. Mol. Cell. 59(2), 298-308 (2015).

    4. Carden, T.R., Correale, J., Pasquini, J.M., et alTransferrin enhances microglial phagocytic capacity. Mol. Neurobiol. 56(9), 6324-6340 (2019).

    5. Li, H., Rybicki, A.C., Suzuka, S.M., et alTransferrin therapy ameliorates disease in β-thalassemic mice. Nat. Med. 16(2), 177-182 (2010).