A3641
Apoferritin from equine spleen
0.2 μm filtered
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Form:
liquid
Mol wt:
major subunit ML 19,889, minor subunit MH 22,200, native ~481.2 kDa (24 subunits, approx. 20 kDa each)
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Permítanos ayudarlesterility
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
Quality Level
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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.
Clase de almacenamiento
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves
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Ferritin-iron increases killing of Chinese hamster ovary cells by X-irradiation
Nelson JM and Stevens RG
Cell proliferation, 25(6), 579-585 (1992)
Visualizing macromolecular complexes with in situ liquid scanning transmission electron microscopy
Evans JE, et al.
Micron (Oxford, England : 1993), 43(11), 1085-1090 (2012)
Jan-Philip Wieferig et al.
IUCrJ, 8(Pt 2), 186-194 (2021-03-13)
As cryo-EM approaches the physical resolution limits imposed by electron optics and radiation damage, it becomes increasingly urgent to address the issues that impede high-resolution structure determination of biological specimens. One of the persistent problems has been beam-induced movement, which
M J MacDonald et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 8(10), 777-781 (1994-07-01)
In screening a rat pancreatic islet cDNA library by differential hybridization for transcripts increased by glucose, the H chain of ferritin, an iron storage protein, was identified. An ELISA for rat ferritin showed that the insulin cell contains a surprisingly
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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