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Validated All-in-One™ qPCR Primer for FTL(NM_000146.3) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
This gene encodes the light subunit of the ferritin protein. Ferritin is the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin chains. Variation in ferritin subunit composition may affect the rates of iron uptake and release in different tissues. A major function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in this light chain ferritin gene are associated with several neurodegenerative diseases and hyperferritinemia-cataract syndrome. This gene has multiple pseudogenes. [provided by RefSeq].
Gene References into function
- gene coding and flanking regions were sequenced and examined for mutations that might modulate the iron burden of individuals harboring the common mutant hemochromatosis HFE genotype or cause hemochromatosis independent of mutations in the HFE gene
- Analysis of sequence effect on folding efficiency of ferritin heavy and light subunits.
- The genetic defects in the FTL gene are unlikely to be a common cause of typical PD, at least in a North America population.
- autosomal dominant basal ganglia disorder caused by an adenine insertion at position 460-461 of the gene for ferritin light polypeptide (FTL) in a French family
- Adult-onset generalized dystonia due to a mutation in ferritin, light polypeptide.
- Intra-leukocytic hemosiderin inclusions (a complex of ferritin, denatured ferritin and other material) are associated with iron overload and acute infection.
- Results describe an hereditary ferritinopathy with a novel mutation (C insertion at nt646-647 in exon 4) in the ferritin light chain gene, resulting in a longer than normal protein.
- Results describe the combined effects of DNA transcription and mRNA translation regulation of ferritin-L synthesis.
- Quantitative RNA analysis confirmed down-regulation of ferritin light polypeptide and insulin-like growth factor binding protein 1 in hydatiform mole increased incidence of gestational trophoblastic neoplasia.
- These results demonstrate that, in a human metastatic melanoma cell line, the stress condition promoted by L-ferritin down-modulation, can substantially influence proper maturation of tyrosinase
- X-ray structures of recombinant human L-chain ferritin (HuLF) show a cluster of acidic residues at the ferrihydrite nucleation site and at the iron channel along the threefold axis, and an ordered Cd2+ structure within the iron channel.
- The findings suggest that the pathogenic effects of Ln1 expression are more likely due to deregulation of cellular iron homeostasis rather than to protein conformational problems.
- Demonstrated iron uptake by ferritins into multiple organs. Uptake is greater when iron delivered by H-ferritin compared to L-ferritin.
- FTL is a marker gene useful for stratifying osteosarcoma patients into low- and high-risk groups and predicting therapy outcome.
- We have detected a significant inverse correlation of -0.565 (P<0.0001) between serum ferritin when <50 microg/L and FGF-23.
- metacarpophalangeal arthropathy was independently associated with older age, higher ferritin, the presence of the C282Y +/+ and C282Y/H63D hemochromatosis protein(HFE) genotypes and higher percentage of transferrin saturation.
- FTL and FTH subunits respond independently to cellular iron concentrations
- In exon 4 of the FTL gene, duplication of the 469-484 sequence is found replacing the C-terminal 14 amino acid residues with a novel 23 amino acid sequence.
- placental Ferritin protein expression decreased slightly in mild anemia but significantly in moderate anemia
- the rate of change of serum ferritin in untreated HFE (hemochromatosis protein) C282Y homozygotes is highly variable and may increase or decrease over time
- hereditary ferritinopathy pathogenesis is likely to result from a combination of reduction in iron storage function
