FTL (F4T8H) Rabbit mAb #68106

Ferritin is a ubiquitous and highly conserved protein that plays a major role in iron homeostasis by sequestering and storing iron in a non-toxic and bioavailable form (1). The assembled ferritin molecule, often referred to as a nanocage, can store up to 4,500 atoms of iron (2,3). It forms a holoenzyme of ~450 kDa, consisting of 24 subunits made up of two types of polypeptide chains: ferritin heavy chain (FTH) and ferritin light chain (FTL), each having unique functions. FTHs catalyze the first step in iron storage, the oxidation of Fe(II), whereas FTLs promote the nucleation of ferrihydrite, enabling storage of Fe(III) (4). In addition to iron buffering, FTH also enhances thymidine biosynthesis (5). Serum ferritin levels indicate the amount of iron stored in the body and is the most sensitive test for anemia. It is markedly elevated in inflammation, malignancy, and iron overload disorders (6). Research studies have found that defects in ferritin proteins are also associated with several neurodegenerative diseases (7).

FTL expression is elevated in several malignancies, including gastric (8), breast (9), and prostate (10) cancer. Decreased FTL expression leads to an increase in susceptibility to ferroptotic cell death (11).