FERRITIN, HUMAN Chemical Properties

storage temp. 

2-8°C

form 

saline solution

color 

red to brown

EPA Substance Registry System

Ferritin (9007-73-2)

Safety Information

Hazard Codes 

B,Xn

Risk Statements 

22

RIDADR 

UN 3082 9 / PGIII

WGK Germany 

3

RTECS 

LK0500000

F 

10-21

HS Code 

35040090

MSDS

• Language:English Provider:SigmaAldrich

FERRITIN, HUMAN Usage And Synthesis

Uses

Tool for the study of protein synthesis and regulatory mechanisms.

Uses

Ferritin, cationized from horse spleen has been used:

• to incubate amoebae (10⁶) in the study, to determine whether trophozoites are able to take up ferritin and internalise this protein for their growth in axenic culture
• to determine phagosome-lysosome fusion by electron microscopy
• to label freshly excised chick optic tecta in serum free incubation medium

Uses

Ferritin from human liver has been used as model protein in size-exclusion high-performance liquid chromatography technique and for synthetic nanopore translocation studies. It has also been used to test its effect on the susceptibility of shrimp (Litopenaeus vannamei) to the white spot syndrome virus.

Definition

FERRITIN, HUMAN is a major iron storage protein found in the spleen, liver and intestinal mucosa of vertebrates. It consists of a protein shell surrounding a crystalline, hydrated iron oxide-phosphate core.

General Description

Ferritin, an iron-storage protein is usually present in the liver and spleen in mammals. Iron and?ferritin?are distributed relatively same in the eye. Ferritin is made up of heavy and light chains.

Biochem/physiol Actions

Ferritin holds iron at its ferric state (Fe3+). The core of ferritin?has the capability to hold 4500 iron molecules. It is essential to store iron in vertebrates. Ferritin?is also essential to store and transport iron in invertebrates. It plays a key role in dietary iron absorption.

Purification Methods

The purification of this major iron-binding protein is achieved by homogenisation in water and precipitation with ammonium sulfate, repeating the cycle of ultracentrifugation, and molecular sieve chromatography through a Sephadex 4B column. Isoelectric focusing reveals a broad spectrum of impurities which can be separated by ion-exchange chromatography on Sephadex A-25 and stepwise elution. [Konijn et al. Anal Biochem 144 423 1985.]

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