Recombinant Mouse TfR (Transferrin R) Protein, CF Summary
Cys89-Phe763, with an N-terminal 6-His tag
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Recombinant Mouse TfR (Catalog # 9706-TR) is coated at 5 µg/mL (100 µg/mL), Biotinylated Mouse Holo-Transferrin binds with an ED50 of 0.4-2.4 μg/mL.
Background: TfR (Transferrin R)
The Transferrin Receptor (TfR or TfR-1, designated CD71) is a type II transmembrane glycoprotein expressed on erythroid progenitors, muscle cells and proliferating cells as a 188 kDa disulfide-linked homodimer of 95 kDa monomers (1-4). As the major mediator of cellular iron uptake, it binds and internalizes diferric transferrin, allowing iron release at the low pH of the endosome (2, 5). The mouse TfR cDNA encodes 763 amino acids (aa) including a 67 aa N-terminal intracellular domain, a 21 aa transmembrane domain, and a 675 aa extracellular domain (ECD) with helical, peptidase (nonfunctional), and ligand binding domains, including an RGD potential integrin binding site (5). Mouse TfR ECD shares 76% and 91% aa identity with human and rat, respectively. A cleaved and truncated 85 kDa soluble form of TfR (sTfR) arises from trypsin proteolysis at aa 100, producing the circulating form of TfR (3). sTfR concentration in plasma or serum is proportional to total TfR and can be increased by iron deficiency (3). Erythroid progenitors, which use iron for hemoglobin synthesis, normally account for the bulk of total body TfR production (3). Since rapidly growing cells require iron to replicate DNA, cancer cells can express up to 5-fold more TfR than quiescent cells in the surrounding tissue (2, 4). Antibody targeting of TfR can inhibit tumor cell proliferation and induce apoptosis (2, 4). The hereditary hemochromatosis protein HFE competes with diferric transferrin for binding to TfR, and targets TfR for degradation rather than recycling (2, 5). TfR has been reported to have ferritin-independent functions in T cell development, immunological synapse formation and galectin-3-mediated cell death, and to be a cell entry receptor for New World hemorrhagic fever arenaviruses (2, 4, 6).
- Stearne P.A. et al. (1985) J. Immunol. 134:3474.
- Daniels, T.R. et al. (2006) Clin. Immunol. 121:144.
- Skikne, B.S. (2008) Am. J. Hematol. 83:872.
- Macedo, M.F. and M. deSousa (2008) Inflamm. Allergy Drug Targets 7:41.
- Aisen, P. (2004) Int. J. Biochem. Cell Biol. 36:2137.
- Radoshitzky, S.R. et al. (2007) Nature 446:92.
Citation for Recombinant Mouse TfR (Transferrin R) Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
Acute and Chronic Dosing of a High-Affinity Rat/Mouse Chimeric Transferrin Receptor Antibody in Mice
Authors: DM Castellano, J Sun, J Yang, W Ou, AC Zambon, WM Pardridge, RK Sumbria
Sample Types: Plasma
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