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You are here:Home » Antibodies » Abs to Serum Proteins » Anti -Ferritin

Anti -Ferritin

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Specifications

Clone Host Grade Applications
Monoclonal Mouse Affinity Purified E B
Elemental iron is required for a variety of normal cellular functions and vital for proper growth and development. Natural iron is quite insoluble. Excess iron is harmful. 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), 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. 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 (~21kD; 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, where '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. FTH subunit (rich in human heart) is located on chromosome 11. Ferritin is capable of storing up to 4500 atoms of ferric iron. The H:L ratio within ferritin varies in a tissue-specific manner. This ratio 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. L-chains assist in core formation.
Catalog #F4015-17D
ApplicationsSuitable for use in ELISA and Western Blot. Other applications not tested.
Recommended DilutionWestern Blot: 1:1000-1:5000 (ECL).
ELISA: 0.5-1ug/ml. Control protein (F4015-17L) can be used to coat ELISA plates at 1ug/ml.
Optimal dilutions to be determined by the researcher.-
Storage and StabilityMay be stored at 4°C for short-term only. For long-term storage, aliquot and store at -20°C. Aliquots are stable for at least 12 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.
Clone TypeMonoclonal
IsotypeIgG
Clone No3H20
HostMouse
SourceHuman
Concentration~1mg/ml
FormSupplied as a liquid in PBS, pH 7.4, 0.05% sodium azide.
PurityPurified by Protein A/G affinity chromatography.
ImmunogenPurified human liver ferritin ( 95%).
SpecificityRecognizes human liver ferritin. Crossreacts with spleen ferritin.
May crossreact with mouse and rat ferritin. Does not recognize human heart ferritin.
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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