Ferritin consists of homogenous protein segment called as apoprotein and an iron segment which binds to the apoprotein. It is composed of heavy (H) and light (L) chains.
Ferritin is the storage form of iron in mammals, found mainly in liver, bone marrow and spleen. It is also present in small intestine, placenta, kidney and heart. Horse spleen ferritin is made up of 24 identical subunits. Ferritin of different organs is distinct with different electrophoretic mobility and possible functional differences. .
Specificity
The antibody specifically recognizes ferritin from horse spleen.
Immunogen
Purified horse spleen ferritin
Application
Anti-Horse Spleen Ferritin antibody was used for immunocytochemistry of rat brain sections at a working antibody dilution of 1:2000 and in mouse brain sections at 1:1000. The antibody was used for immunoblotting using cell lysates of mouse primary erythroblasts and human ovarian carcinoma cells and human bronchial epithelial cells at a working dilution of 1:1000. The antibody is suitable for immunoelectrophoresis.
Horse Spleen Ferritin antibody has been used:
immunofluorescence
in western blotting
in immunohistochemistry
Biochem/physiol Actions
Ferritin iron is oxidized from Fe(II) to Fe(III) in the presence of the enzyme ferroxidase.
Physical form
Lyophilized from 0.01 M sodium phosphate, 0.015 M sodium chloride, pH 7.2
Reconstitution
Reconstitute with 0.135 M sodium chloride.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Iron accumulation in the brain has been associated with neurodegenerative disorders, including epilepsy. In our previous SAGE study, we showed that ferritin, an iron-storage protein, was one of the genes (Ferritin-H) that showed overexpression before the chronic epileptic phase. In
Biocompatibility of ferritin-based nanoparticles as targeted MRI contrast agents
Charlton J R, et al.
Nanomedicine: Nanotechnology, Biology, and Medicine, 12(6), 1735-1745 (2016)
Terminal erythropoiesis is accompanied by extreme demand for iron to ensure proper hemoglobinization. Thus, erythroblasts must modify the "standard" post-transcriptional feedback regulation, balancing expression of ferritin (Fer; iron storage) versus transferrin receptor (TfR1; iron uptake) via specific mRNA binding of
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