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Item No. 32032

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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; Item No. 32033) to ferritin light chains (FTLs). 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. FTL is overexpressed in acute myeloid leukemia and leukemic stem cells compared with normal hematopoietic stem cells.4 Nucleotide duplications in FTL are associated with neuroferritinopathy, an autosomal dominant neurodegenerative disease characterized by the presence of intracellular ferritin inclusion bodies and iron accumulation in glia and neurons throughout the CNS.3 Point mutations in the 5’-UTR of FTL have been found in individuals with hereditary hyperferritinemia-cataract syndrome.5 Cayman’s Ferritin Light Chain (human, recombinant) protein consists of 191 amino acids and has a calculated molecular weight of 22.1 kDa.
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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 light chain gene mutation in a large Australian family with hereditary hyperferritinemia-