Recombinant Transferrin Receptor/TFRC/CD71 Monoclonal Antibody (AN300360P)
For research use only.
| Verified Samples |
Verified Samples in WB:?TFRC konckout Hela, Hela Verified Samples in IP: Jurkat |
| Dilution | WB 1:500-1:2000, IP 0.5-2 μL/mg of lysate |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human |
| Applications | WB, IP |
| Clonality | Monoclonal |
| Immunogen | Recombinant Human Transferrin Receptor/TFRC/CD71 protein |
| Abbre | TFRC |
| Synonyms | IMD, sTfR, transferrin receptor protein, TFRC, CD71, IMD46, T9, TFR, TFR1, TR, TRFR, p90, transferrin receptor, sTfR1, transferrin receptor protein 1, T9 |
| Swissprot | |
| Calculated MW | 84 kDa |
| Observed MW |
95 kDa
The actual band is not consistent with the expectation.
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Cell membrane, Melanosome, Secreted |
| Concentration | 1 mg/mL |
| Buffer | 0.2 μm filtered solution in PBS |
| Purification Method | Protein A |
| Research Areas | Cardiovascular, Immunology, Stem Cells, Cancer, Metabolism |
| Clone No. | 12G8 |
| Conjugation | Unconjugated |
| Storage | This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles. |
| Shipping | Ice bag |
| background | 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. 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. 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. Most soluble TfR (sTfR) arises from trypsin proteolysis at aa 100, producing the circulating form of TfR. sTfR concentration in plasma or serum is proportional to total TfR and can be increased by iron deficiency. Erythroid progenitors, which use iron for hemoglobin synthesis, normally account for the bulk of total body TfR production. 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. Antibody targeting of TfR can inhibit tumor cell proliferation and induce apoptosis. The hereditary hemochromatosis protein HFE competes with diferric transferrin for binding to TfR, and targets TfR for degradation rather than recycling. 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. |
Other Clones
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Other Formats
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Unconjugated
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