Recombinant mouse Transferrin protein (His tag) is a Mouse Full Length protein, in the 1 to 697 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
Trf, Tf, Serotransferrin, Transferrin, Beta-1 metal-binding globulin, Siderophilin
Recombinant mouse Transferrin protein (His tag) is a Mouse Full Length protein, in the 1 to 697 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS.
The ED50 for this effect is typically 0.05-0.2 μg/mL.
pH: 7.4
Constituents: 100% PBS
Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
Belongs to the transferrin family.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Transferrin also known as serotransferrin or siderophilin is a glycoprotein with a mass of approximately 80 kDa. It is primarily synthesized in the liver and subsequently secreted into the bloodstream. Transferrin has an important role in iron transport and maintains iron homeostasis by binding and delivering iron to various tissues throughout the body. It can bind two ferric ions (Fe3+) in association with an anion usually bicarbonate. In biological fluids transferrin exists in serum plasma and other extracellular fluids.
Transferrin facilitates the transportation of iron ions. It delivers iron to cells by binding to transferrin receptors on cell surfaces forming a complex that gets internalized via receptor-mediated endocytosis. Inside the endosomes acidic conditions cause iron to release from transferrin enabling its utilization in cellular processes like DNA synthesis and electron transport. Transferrin itself acts independently and does not form part of a larger protein complex. Variants of transferrin include mouse transferrin bovine transferrin and biotinylated transferrin each with similar function across different species.
Transferrin operates centrally in iron metabolism and homeostasis pathways. It functions in coordination with the transferrin receptor 1 (TfR1) which facilitates cellular uptake of the transferrin-iron complex. Additionally transferrin plays a role in the hepcidin regulatory pathway. Hepcidin modulates iron homeostasis by decreasing iron absorption in the intestine and controlling iron release from macrophages and hepatocytes. Transferrin's ability to bind iron connects it to other iron-containing proteins such as ferritin which stores excess iron in cells.
Several iron-related conditions can impact transferrin function including anemia and hemochromatosis. Anemia often occurs when there is insufficient iron delivery leading to inadequate hemoglobin synthesis and reduced oxygen transport. Aberrant transferrin receptor activity affects iron uptake in such conditions. Hemochromatosis characterized by iron overload can occur due to mutations in genes like HFE leading to changes in hepcidin regulation and increased intestinal iron absorption. Transferrin levels and saturation are clinical indicators used to assess iron status in such diseases.
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Measured in a serum-free cell proliferation assay using MCF-7 human breast cancer cells.
The ED50 for this effect is typically 0.05-0.2 μg/mL.
SDS-PAGE analysis of ab276933
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