Human Holo-Transferrin Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Human Holo-Transferrin Protein, CF Summary

Details of Functionality
Measured in a serum-free cell proliferation assay using MDCK canine kidney epithelial cells. Taub, M. et al. (1979) PNAS 76:3338. The ED50 for this effect is 0.075-0.375 μg/mL.
Optimal concentration depends on cell type as well as the application or research objectives.
Source
Human plasma-derived Holo-Transferrin protein

The human plasma used for the isolation of this product were certified by the supplier to be HIV-1 and HBsAg negative at the time of shipment. Human blood products should always be treated in accordance with universal handling precautions.

Protein/Peptide Type
Natural Proteins
Gene
TF
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

SDS-PAGE
76-81 kDa, reducing conditions
Publications
Read Publications using
2914-HT in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in NH4HCO3.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 20 mg/mL in sterile, deionized water.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Human Holo-Transferrin Protein, CF

  • HoloTransferrin
  • Holo-Transferrin

Background

Human Transferrin (Tf) is a single chain, 80 kDa member of the anion-binding superfamily of proteins (1 - 5). It is a bilobed molecule that is the product of an ancient gene duplication event (1, 6). Transferrin is synthesized as a 698 amino acid (aa) precursor that is divided into a 19 aa signal sequence plus a 679 aa mature segment that contains 19 intrachain disulfide bonds. The crystal structure of Tf reveals a protein with two flanking 340 aa globular domains. Each are composed of a beta -sheet surrounded by series of alpha -helices (1, 7). The N- and C-terminal flanking regions (or domains) will bind ferric iron through the interaction of an obligate anion (usually bicarbonate) and four amino acids (His, Asp, and two Tyr) (7, 8). Apotransferrin (or iron‑free) will initially bind one atom of iron at the C-terminus, and this is followed by subsequent iron binding by the N‑terminus to form holotransferrin (diferric Tf) (8, 9). Through its C-terminal iron‑binding domain, holotransferrin will interact with the type I Tf receptor (TfR) on the surface of cells where it is internalized into acidified endosomes. Iron dissociates from the Tf molecule within these endosomes, and is transported into the cytosol as ferrous iron. At physiological pH, iron‑free apotransferrin is not bound by TfR. But at acidic pH, such as exists in the endosome, apotransferrin has considerable affinity for TfR. Thus, it remains bound to TfR and is recycled back to the cell surface where a neutral pH environment dissociates ligand from receptor. Each Tf molecule recycles 100 - 150 times during its lifetime (8 - 11). In addition to TfR, transferrin is reported to bind to cubulin, IGFBP3, microbial iron‑binding proteins and liver-specific TfR2 (7, 12, 13, 14). Transferrin is variably glycosylated and the degree of sialylation is suggestive of certain clinical conditions (15). Finally, Tf is highly allelic and the gene codominant, with many single aa changes noted. Three general forms are known, based on standard electrophoretic mobility. Fast Tf is known as transferrin B, slow transferrin is transferrin D, and the middle migrating transferrin is type/variant C, thre most common (16, 17). Mature human TF is 73% aa identical to both mouse and rat Tf, and 68% and 71% aa identical to bovine and equine Tf, respectively.

  1. Brus, C.M. et al. (2001) Nat. Struct. Biol. 4:919.
  2. Schaeffer, E. et al. (1987) Gene 56:109.
  3. MacGillivray, R.T.A. et al. (1983) J. Biol. Chem. 258:3543.
  4. Yang, F. et al. (1984) Proc. Natl. Acad. Sci. USA 81:2752.
  5. Uzan, G. et al. (1984) Biochem. Biophys. Res. Commun. 119:273.
  6. Zak, O. et al. (2002) Biochemistry 41:7416.
  7. Gomme, P.T. and K. B. McCann (2005) Drug Discov. Today 10:267.
  8. Liu, R. et al. (2003) Biochemistry 42:12447.
  9. Pakdaman, R. et al. (1999) J. Mol. Biol. 293:1273.
  10. Hemadi, M. et al. (2004) Biochemistry 43:1736.
  11. Aisen, P. et al. (2001) Int. J. Biochem. Cell Biol. 33:940.
  12. Kozyraki, R. et al. (2001) Proc. Natl. Acad. Sci. USA 98:12941.
  13. Boulton, I.C. et al. (1998) Biochem. J. 334:269.
  14. Robb, A. and M. Wessling-Resnick (2004) Blood 104:4294.
  15. Landberg, E. et al. (1995) Biochem. Biophys. Res. Commun. 210:267.
  16. Gorg, A. et al. (1983) Hum. Genet. 64:222.
  17. Bean, P. and J.B. Peter (1994) Clin. Chem. 40:2078.

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Publications for Holo-Transferrin (2914-HT)(7)

We have publications tested in 2 confirmed species: Human, Mouse.

We have publications tested in 3 applications: Bioassay, Cell Culture, In Vivo.


Filter By Application
Bioassay
(4)
Cell Culture
(1)
In Vivo
(2)
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Filter By Species
Human
(5)
Mouse
(2)
All Species
Showing Publications 1 - 7 of 7.
Publications using 2914-HT Applications Species
RM Martin, K Ikeda, MK Cromer, N Uchida, T Nishimura, R Romano, AJ Tong, VT Lemgart, J Camarena, M Pavel-Dinu, C Sindhu, V Wiebking, S Vaidyanath, DP Dever, RO Bak, A Laustsen, BJ Lesch, MR Jakobsen, V Sebastiano, H Nakauchi, MH Porteus Highly Efficient and Marker-free Genome Editing of Human Pluripotent Stem Cells by CRISPR-Cas9 RNP and AAV6 Donor-Mediated Homologous Recombination Cell Stem Cell, 2019;24(5):821-828.e5. 2019 [PMID: 31051134] (Cell Culture, Human) Cell Culture Human
K Denis, M Le Bris, L Le Guennec, JP Barnier, C Faure, A Gouge, H Bouzinba-S, A Jamet, D Euphrasie, B Durel, N Barois, P Pelissier, PC Morand, M Coureuil, F Lafont, O Join-Lambe, X Nassif, S Bourdoulou Targeting Type IV pili as an antivirulence strategy against invasive meningococcal disease Nat Microbiol, 2019;0(0):. 2019 [PMID: 30911127] (In Vivo, Mouse) In Vivo Mouse
S Poldee, C Metheetrai, S Nugoolsuks, J Frayne, K Trakarnsan Optimization of an erythroid culture system to reduce the cost of in vitro production of red blood cells MethodsX, 2018;5(0):1626-1632. 2018 [PMID: 30560064] (Bioassay, Human) Bioassay Human
BM Hopkinson, C Desler, M Kalisz, PS Vestentoft, L Juel Rasmu, HC Bisgaard Bioenergetic Changes during Differentiation of Human Embryonic Stem Cells along the Hepatic Lineage Oxid Med Cell Longev, 2017;2017(0):5080128. 2017 [PMID: 28265337] (Bioassay, Human) Bioassay Human
Experimental evidences of human coronary microvasculature and myocardial tissue bacterial colonization during meningococcemia Infect Immun, 2016;0(0):. 2016 [PMID: 27481255] (In Vivo, Mouse) In Vivo Mouse
Huang X, Wang Y, Yan W, Smith C, Ye Z, Wang J, Gao Y, Mendelsohn L, Cheng L Production of Gene-Corrected Adult Beta Globin Protein in Human Erythrocytes Differentiated from Patient iPSCs After Genome Editing of the Sickle Point Mutation. Stem Cells, 2015;33(5):1470-9. 2015 [PMID: 25702619] (Bioassay, Human) Bioassay Human
Staquicini FI, Ozawa MG, Moya CA, Driessen WH, Barbu EM, Nishimori H, Soghomonyan S, Flores LG, Liang X, Paolillo V, Alauddin MM, Basilion JP, Furnari FB, Bogler O, Lang FF, Aldape KD, Fuller GN, Höök M, Gelovani JG, Sidman RL, Cavenee WK, Pasqualini R, Arap W Systemic combinatorial peptide selection yields a non-canonical iron-mimicry mechanism for targeting tumors in a mouse model of human glioblastoma. J. Clin. Invest., 2011;121(1):161-73. 2011 [PMID: 21183793] (Bioassay, Human) Bioassay Human

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Bioinformatics

Gene Symbol TF