Elemental iron is required for a variety of normal cellular functions and vital for proper growth and development.
However, natural iron is quite insoluble and excess iron is harmful, since it can catalyze the formation of potentially damaging reactive oxygen species.
Therefore, cells have developed mechanisms to improve solubility of iron and to control intracellular iron levels.
The major pool of body iron (~85%; 40-50 mg/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 (~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 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.
Purified human spleen ferritin was used as immunogen to produce antibodies in rabbits.
Applications:Suitable for use in ELISA, Western Blotting.
Other applications not tested.
Recommended Dilution:Western Blot: 1:1000-1:5000 antibody using ECL.
ELISA: Control protein can be used to coat ELISA plates at 1ug/ml and detected with antibodies (1:10-50K for neat serum and 0.5-1ug/ml for affinity pure).
Optimal dilutions to be determined by the researcher.
Storage and Stability:May be stored at 4°C for short-term only.
For long-term storage and to avoid repeated freezing and thawing, aliquot and add glycerol (40-50%).
Freeze 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.
仕様
Size：100ul
Host：rabbit
Source Antibody：human
Grade：Serum
Purity：Serum.
Form：Supplied as a lyophilized powder from PBS, pH 7.4, 0.05% sodium azide. Reconstitute with 100ul sterile dH2O.
Specificity：Ferritins are quite conserved among various species. The antibody may crossreact with ferritin from mouse, rat and other species. Ferritin from spleen is enriched in "L subunit". However, the antibody specificity with "H subunit has not been studied.
