Product Description
Size: 100µg
Anti-Transferrin antibody (ab82411) is a rabbit polyclonal antibody detecting Transferrin in Western Blot, IP, IHC-P, ICC/IF . Suitable for Dog, Guinea pig, Human, Mouse, Rat . - Over 50 publications - Trusted since 2009
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Rat, Human, Guinea pig, Mouse, Dog,
Applications:IHC-P, IP, ICC/IF, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Full Length Protein corresponding to Human TF. The exact immunogen used to generate this antibody is proprietary information.P02787
Product details:
What is this antibody validated in?
Anti-Transferrin antibody (ab82411) is a rabbit polyclonal antibody and is validated for use in Western Blot (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC-P), Immunocytochemistry/immunofluorescence (ICC/IF) in Dog, Guinea pig, Human, Mouse, Rat samples.
What is the molecular weight of Transferrin?
Anti-Transferrin (ab82411) specifically detects a band for Transferrin (UniProt: P02787) at a molecular weight of 77kDa.
Trusted by the scientific community
Anti-Transferrin (ab82411) was first used in a scientific publication in 2009 and has been cited over 50 times in peer-reviewed journals.
Reviewed by scientists
Anti-Transferrin (ab82411) has over 5 independent reviews from customers.
Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-Preservative: 0.09% Sodium azideConstituents: PBS, 50% Glycerol (glycerin, glycerine), Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
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.
Biological function summary
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.
Pathways
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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Collaboration
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