F4503
Ferritin from equine spleen
Type I, saline solution
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About This Item
Form:
saline solution
Mol wt:
H subunit ~21 kDa, L subunit ~19 kDa
sterility
sterile-filtered
Quality Level
type
Type I
form
saline solution
mol wt
H subunit ~21 kDa, L subunit ~19 kDa
color
red to brown
cation traces
Cd: ≤1% (as % of ferritin)
storage temp.
2-8°C
General description
A shell of 24 protein subunits (apoferritin) and a core Fe 3+ ions with a peptide MW of 440 kDa. Review of the ferritin-like superfamily of iron-storage proteins, virtually ubiquitous in life on earth.
Application
Ferritin from equine spleen has been used:
- in mycobacterial growth assay
- in size-exclusion chromatography
- in labeling of macrophage cells
- as a reference standard in muon spin spectroscopy
Biochem/physiol Actions
A ubiquitous iron storage protein that plays a key role in iron metabolism. It serves as an intracellular iron reserve (particularly in spleen, liver, intestinal mucosa, and bone marrow) and functions in iron detoxification.
A ubiquitous iron storage protein that plays a key role in iron metabolism. It serves as an intracellular iron reserve (particularly in spleen, liver, intestinal mucosa, and bone marrow) and functions in iron detoxification. Studies have shown that ferritin iron incorporation is mediated by a ferroxidase activity associated with ferritin H subunits and a nucleation center associated with ferritin L subunits. Release of iron from ferritin has an essential role in iron-dependent lipid peroxidation and may contribute to free radical-induced cell damage in vivo. Therefore, by binding iron, ferritin may function as an antioxidant.
Storage Class
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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Human-brain ferritin studied by muon spin rotation: a pilot study
Bossoni L, et al.
Journal of Physics. Condensed Matter : An Institute of Physics Journal, 29(41), 415801-415801 (2017)
Italo Moglia et al.
Journal of inorganic biochemistry, 183, 184-190 (2017-12-28)
Ferritin is a globular protein that consists of 24 subunits forming a hollow nanocage structure that naturally stores iron oxyhydroxides. Elimination of iron atoms to obtain the empty protein called apoferritin is the first step to use this organic shell
The effectiveness of ferritin as a contrast agent for cell tracking MRI in mouse cancer models
Lee CW, et al.
Yonsei Medical Journal, 58(1), 51-58 (2017)