Ferritin comprises 24-subunit and belongs to the ferritin-like diiron-carboxylate protein superfamily. Ferritin exists as heavy (H) and light (L) subunits. Liver ferritin is majorly L subunit and the spleen has the H submit. The L subunit is mapped to human chromosome 9q13.33 and the H subunit 11q12.3.
Ferritin from human liver has been used as model protein in size-exclusion high-performance liquid chromatography technique and for synthetic nanopore translocation studies. It has also been used to test its effect on the susceptibility of shrimp (Litopenaeus vannamei) to the white spot syndrome virus.
A ubiquitous iron storage protein that plays a key role in iron metabolism. It serves as an intracellular iron reserve (particularly in spleen, liver, intestinal mucosa, and bone marrow) and functions in iron detoxification. Studies have shown that ferritin iron incorporation is mediated by a ferroxidase activity associated with ferritin H subunits and a nucleation center associated with ferritin L subunits. Release of iron from ferritin has an essential role in iron-dependent lipid peroxidation and may contribute to free radical-induced cell damage in vivo. Therefore, by binding iron, ferritin may function as an antioxidant.
Ferritins are part of the host defense system and play a role in response to viral infection in animals. The abnormal levels of ferritin are correlated to many tumors associated with the prostate, breast and brain. High levels of ferritin are implicated in inflammation and macrophage activation syndrome (MAS). Mutations in the light subunit chain can lead to the neurodegenerative disease, hereditary ferritinopathy.
Solution in 10 mM Tris, 150 mM NaCl, pH 8.0, and 0.1% sodium azide.