Ferritin, Liver, Human, Western Blot Control

Western Blot Control for F4015-17D.\n\nElemental 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.\n\nApplications: \nSuitable for use in Western Blot. Other applications not tested.\n\nRecommended Dilution:\nWestern Blot: 10ul/lane. Ready to use.\nOptimal dilutions to be determined by researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage, aliquot and store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees 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.

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SPECIFICATIONS

Catalog Number

F4015-17L

Size

50ul

Applications

WB

Form

Supplied as a liquid in denaturing SDS-PAGE sample buffer

Purity

Highly purified ((same/more than) 95%).

References

1. Harrsion, P.M., et al., BBA 1275: 161-203 (1996). 2. Picard, V., et al., JBC 273: 15382-15386 (1998). 3. Rucker, P-F., et al., JBC 271: 33352-33357 (1996). 4. Nelson, N., et al., EMBO J. 18: 4361-4371 (1999) (review). 5. Cairo, G., et al., Biochem. J. 352: 241-250 (2000).