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Validated All-in-One™ qPCR Primer for FTH1(NM_002032.2) Search again
Product ID:
HQP006439
(click here to view gene annotation page)
Species:
Human
Symbol:
Alias:
FHC, FTH, FTHL6, HFE5, PIG15, PLIF
Gene Description:
ferritin heavy chain 1
Target Gene Accession:
NM_002032.2(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
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 heavy subunit of ferritin, the major intracellular iron storage protein in prokaryotes and eukaryotes.
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
- An alternative model of H ferritin promoter transactivation by c-Jun (H ferritin, also called isoferritin)
- activates regulatory T cells by induction of changes in dendritic cells
- mu-1,2-Peroxobridged di-iron(III) dimer formation in human H-chain ferritin
- Analysis of sequence effect on folding efficiency of ferritin heavy and light subunits.
- FTH expression is mediated by Nrf2 in response to xenobiotics and cancer chemopreventive dithiolethiones
- Placenta immunomodulatory ferritin (PLIF) plays a major role in placentation and embryonic growth.
- Intra-leukocytic hemosiderin inclusions (a complex of ferritin, denatured ferritin and other material) are associated with iron overload and acute infection.
- Data reveal striking differences in iron oxidation and hydrolysis chemistry between human mitochondrial ferritin and human H-chain ferritin despite their similar diiron ferroxidase centers
- H-ferritin mRNA, IL-1beta, and poly(C)-binding proteins may have roles in ferritin translation and iron homeostasis in human liver
- We report the crystallographic structures of four human H apoferritin variants at a resolution of up to 1.5 Angstrom. Crystal derivatives using Zn(II) as redox-stable alternative for Fe(II), allows us to characterize the different metal-binding sites.
- H ferritin regulates folate metabolism through its internal ribosome entry site
- We have detected a significant inverse correlation of -0.565 (P<0.0001) between serum ferritin when <50 microg/L and FGF-23.
- FTL and FTH subunits respond independently to cellular iron concentrations
- C. albicans can exploit iron from host ferritin via morphology dependent binding through Als3
- ferritin binds to HKa (cleaved high molecular weight kininogen) with high affinity (K(d) 13 nM). Further, ferritin antagonizes the antiangiogenic effects of HKa, enhancing the migration, assembly, and survival of HKa-treated endothelial cells
