The ferritin molecule consists of 24 self-assembling polypeptide subunits composed of the heavy and light chains.

Ferritins (MW: ~ 450 kD) are polymeric proteins composed of 2 subunits a heavy chain and a light chain polypeptide, that reversibly bind and store iron in liver, spleen and bone marrow. The ferritin molecule consists of 24 self-assembling polypeptide subunits composed of the heavy and light chains. Ferritin light chain is the main intracellular iron storage protein. The proportion of heavy and light chain composing the ferritin molecule varies from tissue to tissue. This variation accounts for the differences in the rate of iron uptake and release in different tissues or organs. Recombinant Human Ferritin Light Chain is produced in E.coli as a single non-glycosylated polypeptide having a molecular weight of 19 kDa. Clinically, the monitoring of serum ferritin levels aides in the diagnosis and management of iron metabolic disorders. Serum levels increase in hepatic diseases, various malignancies, inflammation and late stage hemochromatosis. Ferritin levels are also indicative of the erosion of iron stores during pregnancy. Genetic defects in the light chain ferritin gene are linked with several neurodegenerative disorders.

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