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Quality Level
sterility
0.2 μm filtered
form
liquid
mol wt
major subunit ML 19,889
minor subunit MH 22,200
native ~481.2 kDa (24 subunits, approx. 20 kDa each)
color
clear to slightly hazy, solution
storage temp.
2-8°C
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Application
Apoferritin from equine spleen has been used:
- to determine its partition coefficients in phase systems
- in NaCl for iron loading of cultured cells
- in in situ liquid scanning transmission electron microscope for imaging the interface of biology and nanotechnology
Biochem/physiol Actions
This protein shell of ferritin lacking iron is widely used for the calibration of gel filtration columns and sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. It is very abundant in beta-cells of the pancreas where it acts as an anti-oxidant. When added to cultured endothelial cells apoferritin is taken up in a dose-responsive manner and appears to protect the cells from oxidant-mediated cytolysis.
Physical form
Solution in 0.135 M sodium chloride.
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Visualizing macromolecular complexes with in situ liquid scanning transmission electron microscopy
Evans JE, et al.
Micron (Oxford, England : 1993), 43(11), 1085-1090 (2012)
Ferritin-iron increases killing of Chinese hamster ovary cells by X-irradiation
Nelson JM and Stevens RG
Cell proliferation, 25(6), 579-585 (1992)
Cecilia Pozzi et al.
Proceedings of the National Academy of Sciences of the United States of America, 114(10), 2580-2585 (2017-02-17)
X-ray structures of homopolymeric L-ferritin obtained by freezing protein crystals at increasing exposure times to a ferrous solution showed the progressive formation of a triiron cluster on the inner cage surface of each subunit. After 60 min exposure, a fully
Circularly polarized luminescent CdS quantum dots prepared in a protein nanocage.
Masanobu Naito et al.
Angewandte Chemie (International ed. in English), 49(39), 7006-7009 (2010-08-27)
Hamish G Brown et al.
Communications biology, 5(1), 817-817 (2022-08-15)
Ice thickness is arguably one of the most important factors limiting the resolution of protein structures determined by cryo-electron microscopy (cryo-EM). The amorphous atomic structure of the ice that stabilizes and protects biological samples in cryo-EM grids also imprints some
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