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F4503

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Ferritin from equine spleen

Type I, saline solution

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CAS Number:
MDL number:
NACRES:
NA.77

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

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This Item
F7879A3641A3660
mol wt

H subunit ~21 kDa, L subunit ~19 kDa

mol wt

-

mol wt

major subunit ML 19,889, minor subunit MH 22,200, native ~481.2 kDa (24 subunits, approx. 20 kDa each)

mol wt

-

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

sterility

sterile-filtered

sterility

sterile-filtered

sterility

0.2 μm filtered

sterility

-

type

Type I

type

-

type

-

type

-

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. 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 Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Customers Also Viewed

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)
Adipocyte model of Mycobacterium tuberculosis infection reveals differential iron availability to bacilli in the lipid rich caseous environment
Nandy A, et al.
Infection and Immunity, IAI-00041 (2018)
Sella Kim et al.
Journal of molecular biology, 428(24 Pt B), 5007-5018 (2016-11-03)
Iron and oxygen chemistry is mediated by iron proteins for many biological functions. Carboxylate-bridged diiron enzymes including ferritin have the common mechanism of oxygen activation via peroxodiferric intermediates. However, the route for iron uptake and the structural identification of intermediates
Yves Gossuin et al.
Magnetic resonance in medicine, 48(6), 959-964 (2002-12-05)
Ferritin, the iron-storing protein, speeds up proton transverse magnetic relaxation in aqueous solutions. This T(2) shortening is used in MRI to quantify iron in the brain and liver. Current theoretical models underestimate the relaxation enhancement by ferritin at imaging fields

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