Ferritin Light Chain (human, recombinant)

Ferritin is a spherical protein involved in iron storage and biomineralization. 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, Cay-32033) to ferritin light chains (FTLs). FTH1 and FTL are nearly identical in overall conformation but only share approximately 50% sequence homology. 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. 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. Point mutations in the 5'-UTR of FTL have been found in individuals with hereditary hyperferritinemia-cataract syndrome. Cayman's Ferritin Light Chain (human, recombinant) protein consists of 191 amino acids and has a calculated molecular weight of 22.1 kDa.Synonyms: Epididymis Secretory Sperm Binding Protein, Ferritin L-Chain, Ferritin Light Polypeptide-like 3, Ferritin L Subunit, FTL, L Apoferritin, NBIA3, Neurodegeneration with Brain Iron Accumulation 3. Purity: >95% estimated by SDS-PAGE. Endotoxin Testing: <1.0 EU/µg, determined by the LAL endotoxin assay. Source: Active recombinant human N-terminal His-tagged ferritin light chain expressed in E. coli. Amino Acids: 1-175. MW: 22.1 kDa. Formulation: (Request formulation change), Lyophilized from sterile 50 mM Tris, pH 9.5, with 20% glycerol.