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anti-Mouse (Murine) Hephaestin Anticorps:
anti-Rat (Rattus) Hephaestin Anticorps:
anti-Human Hephaestin Anticorps:
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Human Polyclonal Hephaestin Primary Antibody pour IF (p), IHC (p) - ABIN1715088
Rychtarcikova, Lettlova, Tomkova, Korenkova, Langerova, Simonova, Zjablovskaja, Alberich-Jorda, Neuzil, Truksa: Tumor-initiating cells of breast and prostate origin show alterations in the expression of genes related to iron metabolism. dans Oncotarget 2016
In mice with mutation of Cp and Heph, iron accumulates in glia, while neurons have low iron levels. Both neurons and glia degenerate and mice become ataxic unless given an iron chelator.
The multicopper ferroxidase (Montrer A2BP1 Anticorps) hephaestin enhances intestinal iron absorption in mice.
Data (including data from studies in knockout mice) suggest that hephaestin and ceruloplasmin (Montrer CP Anticorps) play distinct roles in regulation of gene expression in various regions of the brain and are involved in iron homeostasis.
Cp and Heph are necessary for iron export from the retina but are not essential for iron import into the retina.
results show that Heph is expressed by oligodendrocytes and plays an important role in iron efflux from these cells.
Hephaestin and Ireg1 (Montrer SLC40A1 Anticorps) expression respond to systemic rather than local signals of iron status.
Hephaestin has both amine oxidase (Montrer MAOA Anticorps) and ferroxidase (Montrer CP Anticorps) activity primary intestinal enterocytes and may facilitate iron export from intestinal enterocytes; also activity and structural studies of truncated Heph in sla mice
Ceruloplasmin (Montrer CP Anticorps) ane hephaestin are critical for CNS iron homeostasis and that loss of Cp and Heph in the mouse leads to age-dependent retinal neurodegeneration.
CDX2 (Montrer CDX2 Anticorps) expression was modulated in response to changes in intracellular iron levels, implying a regulatory pathway in which increased iron levels lead to increased expression of CDX2 (Montrer CDX2 Anticorps) and HEPH and enhanced iron export.
Copper is required for the proper processing and/or stability of hephaestin.
This review describes function of hephaestin as ferroxidase (Montrer CP Anticorps) is essential for iron binding to apotransferrin in the lamina propria of the intestinal mucosa, a process that is important for further transport of iron to the liver by the portal vein.
Iron efflux from human brain microvasculature endothelial cells ferroportin (Montrer SLC40A1 Anticorps) requires the action of an exocytoplasmic ferroxidase (Montrer CP Anticorps) which can be either endogenous hephaestin or extracellular ceruloplasmin (Montrer CP Anticorps).
Heph is active in placenta but may not play a key role in placental iron transport.
These results support the hypothesis that hephaestin is involved in iron mobilization of iron from the intestine to circulation.
In contrast to ceruloplasmin (Montrer CP Anticorps), hephaestin was incapable of direct oxidation of adrenaline and dopamine implying a difference in biological substrate specificities between these two homologous ferroxidases.
Hephaestin is expressed in enterocytes, in the antral portion of the stomach, in the myenteric and submucous plexi, and in pancreatic beta-cells.
The gene structure, spanning approximately 100 kb, was assembled from the cDNA clones and the chromosome X genomic sequence data. Modelling supports its role as a membrane-tethered ferroxidase (Montrer CP Anticorps).
The hephaestin protein mRNA expression is not significantly altered by variations in iron homeostasis. The effect of phlebotomy-induced erythropoiesis did not alter either gene transcript mRNA expression.
Reombinant hephaestin was shown to have both multicopper oxidase and ferroxidase (Montrer CP Anticorps) activity.
Results suggest the possibility that FPN-1 (Montrer SLC40A1 Anticorps) might associate and interact with Heph in the process of iron exit across the basolateral membrane of intestinal absorptive cell.
The protein encoded by this gene is similar to an iron transport protein found in mouse. The mouse protein is similar to ceruloplasmin, a serum multi-copper ferroxidase, and is thought to be a membrane-bound protein responsible for transport of dietary iron from epithelial cells of the intestinal lumen into the circulatory system. In mouse, defects in this gene can lead to severe microcytic anemia. Three transcript variants encoding different isoforms have been described for this gene.
, sex linked anemia