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Item No. 32033

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Ferritin is a spherical protein involved in iron storage and biomineralization.1,2 It is primarily localized to the cytoplasm, but is also present in the mitochondria and nucleus, and is composed of 24 protein subunits with a tissue-specific ratio of ferritin heavy chains (FTH1s) to ferritin light chains (FTLs; Item No. 32032). FTH1 and FTL are nearly identical in overall conformation but only share approximately 50% sequence homology.3 FTH1 functions as a ferroxidase that catalyzes the oxidation of Fe(II) to Fe(III) and FTL has roles in iron nucleation and protein stability. FTH1 is overexpressed in acute myeloid leukemia and leukemic stem cells compared with normal hematopoietic stem cells.4 Elevated levels of cytoplasmic and nuclear FTH1 are associated with a favorable and poor prognosis, respectively, in patients with triple negative breast cancer.5 Point mutations in the 5’-UTR of FTH1 mRNA have been found in individuals with autosomal dominant iron overload.6 Disruption of Fth1 is embryonic lethal in mice.7 Cayman’s Ferritin Heavy Chain (human, recombinant) protein consists of 183 amino acids and has an apparent molecular mass of 21.2 kDa by SDS-PAGE under reducing conditions.
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1. Ferritin light-
2. Ferritin light chain confers protection against sepsis-
3. A mutant light-
4. Ferritin heavy/light chain (FTH1/FTL) expression, serum ferritin levels, and their functional as well as prognostic roles in acute myeloid leukemia. Eur. J. Haematol. 102(2), 131-142 (2019).
5. Ferritin heavy chain in triple negative breast cancer: A favorable prognostic marker that relates to a cluster of differentiation 8 positive (CD8+) effector T-
6. A mutation, in the iron-
7. Early embryonic lethality of H ferritin gene deletion in mice. The Journal of Biological Chemisty 275(5), 3021-3024 (2000).