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You are here:Home » Molecular Biology » MB-Serum Proteins » Ferritin, Spleen, Human

Ferritin, Spleen, Human


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Catalog #F4015-11D
DescriptionElemental iron is required for a variety of normal cellular functions and vital for proper growth and development. Natural iron is quite insoluble and excess iron is harmful, since it can catalyze the formation of potentially damaging reactive oxygen species. Cells have developed mechanisms to improve solubility of iron and to control intracellular iron levels. The major pool of body iron (~85%; 40-50mg/kg) is found in circulating hemoglobin and muscle myoglobin. Iron absorption occurs primarily in the intestine (duodenum) and inversely related to body iron reserve. Several proteins including Ferritin, transferrin (Tf), transferrin receptors (TfRs), and iron regulatory proteins (IRPs) etc play a key role in iron metabolism. Ferritin is the major protein involved in iron sequestration and detoxification. Ferritin is found in all living species and its three dimensional structure is conserved in all species despite very low sequence identity from bacteria to human. Mammalian liver and spleen ferritin (~450kD) consists of 24 subunits of 2 species, the heavy subunit (~2kD; FTH) and the light subunit (~ 19kD; FTL). The 2 types of apoferritin subunits were designated H and L for heart and liver, respectively. Ferritin molecules from plants and bacteria contain only H-type chains. ‘H-type’ is associated with the presence of centers catalyzing the oxidation of two Fe(II) atoms. FTL subunit (rich in human liver and spleen) is coded by a gene in segment 19q13.3 and FTH subunit (rich in human heart) is located on chromosome 11. Ferritin is capable of storing up to 4,500 atoms of ferric iron. The H-to-L ratio within ferritin varies in a tissue- specific manner and is also influenced by pathophysiological conditions, including inflammation and malignancy. Hyperferritinemia- cataract syndrome has a mutation in the iron response element (IRE) in the 5-prime noncoding region of the FTL gene. Synthesis of both ferritin subunits is controlled by a common cytosolic protein, iron regulatory proteins (IRPs), which binds to the iron- responsive element (IRE) in the 5'-UTR of the H-and L-ferritin mRNAs. H-chains are important for Fe(II) oxidation and L-chains assist in core formation.
ApplicationsSuitable for use in Western Blot. Other applications not tested.
Recommended DilutionLoad 10ul/lane
Optimal dilution to be determined by researcher.
Storage and StabilityMay be stored at 4°C for short-term only. For long-term storage, store at -20°C. Aliquots are stable for at least 6 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
SourceHuman spleen ferritin
PurityHighly purified
ConcentrationNot determined.
FormSupplied as a liquid in SDS-PAGE reducing sample buffer.
Important NoteThis product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

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