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

Dilutions
  • Bioactivity
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 sterile water.
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)(43)

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

We have publications tested in 4 applications: Bioassay, Cell Culture, In Vivo, Surface Plasmon Resonance.


Filter By Application
Bioassay
(26)
Cell Culture
(13)
In Vivo
(2)
Surface Plasmon Resonance
(1)
All Applications
Filter By Species
Human
(39)
Mouse
(4)
All Species
Showing Publications 1 - 10 of 43. Show All 43 Publications.
Publications using 2914-HT Applications Species
Wang, Y;Yang, X;Zhang, H;Liu, N;Liu, Y;Gai, Z;Liu, Y;Lv, Y; Generation of a transgene-free iPS cell line (SDQLCHi053-A) from a young girl carrying a heterozygous mutation (c.427C &gt; T) in SYNGAP1 gene Stem cell research 2023-06-07 [PMID: 37385133] (Bioassay, Human) Bioassay Human
Fan, Y;Li, Y;Yang, X;Zhang, H;Wang, B;Guan, J;Gao, J;Ma, X;Liu, Y; Generation and characterization of PBMCs-derived human induced pluripotent stem cell (iPSC) line SDQLCHi051-A from an autism spectrum disorder patient with compound CHD8 gene mutations Stem cell research 2023-06-01 [PMID: 37229974] (Bioassay, Human) Bioassay Human
Martins, GLS;Nonaka, CKV;Rossi, EA;de Lima, AVR;Adanho, CSA;Oliveira, MS;Yahouedehou, SCMA;de Souza, CLEM;Gon�alves, MS;Paredes, BD;Souza, BSF; Evaluation of 2D and 3D Erythroid Differentiation Protocols Using Sickle Cell Disease and Healthy Donor Induced Pluripotent Stem Cells Cells 2023-04-10 [PMID: 37190030] (Bioassay, Human) Bioassay Human
D Ai, X Yang, X Li, N Liu, X Xie, Y Liu, W Song Generation of an induced pluripotent stem cell line SDPHi002-A from a patient with lung cancer Stem Cell Research, 2023-04-15;69(0):103096. 2023-04-15 [PMID: 37104933] (Bioassay, Human) Bioassay Human
M Badat, A Ejaz, P Hua, S Rice, W Zhang, LD Hentges, CA Fisher, N Denny, R Schwessing, N Yasara, NBA Roy, F Issa, A Roy, P Telfer, J Hughes, S Mettananda, DR Higgs, JOJ Davies Direct correction of haemoglobin E beta-thalassaemia using base editors Nature Communications, 2023-04-19;14(1):2238. 2023-04-19 [PMID: 37076455] (Bioassay, Human) Bioassay Human
Y Xi, H Zhang, B Wang, W Song, Y Liu Establishment of an induced pluripotent stem cell line SDQLCHi049-A from a healthy male neonate Stem Cell Research, 2023-04-15;69(0):103097. 2023-04-15 [PMID: 37075622] (Bioassay, Human) Bioassay Human
O Chowdhury, S Ghosh, A Das, H Liu, P Shang, NA Stepicheva, S Hose, D Sinha, S Chattopadh Sustained systemic inflammation increases autophagy and induces EMT/fibrotic changes in mouse liver cells: Protection by melatonin Cellular Signalling, 2022-11-12;101(0):110521. 2022-11-12 [PMID: 36375715] (Cell Culture, Mouse) Cell Culture Mouse
Y Wang, Y Lv, X Yang, Y Li, Z Li, Z Gao, Z Gai, Y Liu Generation of an induced pluripotent stem cell line (SDQLCHi044-A) from a patient with autosomal dominant mental retardation type 5 harboring heterozygous mutation in SYNGAP1 gene Stem Cell Research, 2022-09-17;64(0):102922. 2022-09-17 [PMID: 36183676] (Bioassay, Human) Bioassay Human
J Truch, DJ Downes, C Scott, ER Gür, JM Telenius, E Repapi, R Schwessing, M Gosden, JM Brown, S Taylor, PL Cheong, JR Hughes, DR Higgs, RJ Gibbons The chromatin remodeller ATRX facilitates diverse nuclear processes, in a stochastic manner, in both heterochromatin and euchromatin Nature Communications, 2022-06-17;13(1):3485. 2022-06-17 [PMID: 35710802] (Bioassay, Human) Bioassay Human
CJ Stevens-He, JF Flatt, S Kupzig, LJ Bruce Reticulocyte Maturation and Variant Red Blood Cells Frontiers in Physiology, 2022-03-07;13(0):834463. 2022-03-07 [PMID: 35356079] (Bioassay, Human) Bioassay Human
Show All 43 Publications.

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Bioinformatics

Gene Symbol TF