Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. When human Holo-Transferrin (Catalog # 2914-HT) is coated at 0.5 μg/mL (100 μL/well), the concentration of rhTfR that produces 50% of the optimal binding response is found to be approximately 3-12 ng/mL. |
Source | Mouse myeloma cell line, NS0-derived human TfR (Transferrin R) protein Cys89-Phe760, with an N-terminal 6-His tag |
Accession # | |
N-terminal Sequence | His |
Protein/Peptide Type | Recombinant Proteins |
Gene | TFRC |
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. |
Dilutions |
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Theoretical MW | 76 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 76-85 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in Tris and NaCl with Trehalose. |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions | Reconstitute at 200 μg/mL in PBS. |
The Transferrin Receptor (TfR or TfR-1, designated CD71) is a type 2 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 human TfR cDNA encodes 760 amino acids (aa) including a 67 aa N-terminal intracellular domain, a 21 aa transmembrane domain, and a 672 aa extracellular domain (ECD) with helical, peptidase (nonfunctional), and ligand binding domains, including an RGD potential integrin binding site (5). Human TfR ECD shares 75 - 80% aa identity with mouse, rat, feline, canine, equine, porcine and bovine TfR. A 679 aa alternately spliced form begins at aa 82 and is presumably secreted, while in an 804 aa form, 44 aa are inserted at aa 518 within the peptidase region (6). Most soluble 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, 7).
Transferrin and the blood brain barrier Transferrin, an iron binding protein that facilitates iron uptake in cells, is an integral part of a mechanism that may introduce antibody therapies to the central nervous system. Currently, the brain’s ability to take in antibody therapies i... Read full blog post. |
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