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F6754

Sigma-Aldrich

Ferritin from human liver

Type IV, 10 μg/mL

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About This Item

Numero CAS:
Numero MDL:
Codice UNSPSC:
12352202
NACRES:
NA.61

Origine biologica

human liver

Livello qualitativo

Sterilità

0.2 μm filtered

Tipo

Type IV

Saggio

≥95% (SDS-GE)

Stato

liquid

PM

H subunit ~21 kDa
L subunit ~19 kDa
~440 kDa (a shell of 24 protein subunits (apoferritin) and a core of Fe3+ ions)

Confezionamento

vial of 2 μg

Concentrazione

10 μg/mL

N° accesso UniProt

Temperatura di conservazione

2-8°C

Informazioni sul gene

Descrizione generale

Ferritin comprises 24-subunit and belongs to the ferritin-like diiron-carboxylate protein superfamily. Ferritin exists as heavy (H) and light (L) subunits. Liver ferritin is majorly L subunit and the spleen has the H submit. The L subunit is mapped to human chromosome 9q13.33 and the H subunit 11q12.3.

Applicazioni

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.

Azioni biochim/fisiol

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.
Ferritins are part of the host defense system and play a role in response to viral infection in animals. The abnormal levels of ferritin are correlated to many tumors associated with the prostate, breast and brain. High levels of ferritin are implicated in inflammation and macrophage activation syndrome (MAS). Mutations in the light subunit chain can lead to the neurodegenerative disease, hereditary ferritinopathy.

Stato fisico

Solution in 10 mM Tris, 150 mM NaCl, pH 8.0, and 0.1% sodium azide.

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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Yuan-Hwa Ruan et al.
Fish & shellfish immunology, 28(4), 542-548 (2010-01-05)
We examined the physiological (hemolymph glucose, lactate, and lipid) and innate non-specific immune responses (total hemocyte count (THC), phenoloxidase (PO) activity, respiratory bursts (release of superoxide anion, O(2)(-)) and superoxide dismutase (SOD) activity) to white spot syndrome virus (WSSV) in
P Ruscitti et al.
Clinical and experimental immunology, 191(2), 220-228 (2017-09-30)
Macrophage activation syndrome (MAS) is hyperinflammatory life-threatening syndrome, associated typically with high levels of serum ferritin. This is an iron storage protein including heavy (H) and light (L) subunits, categorized on their molecular weight. The H-/L subunits ratio may be
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This study examined whether a change infrequency of administration of erythropoietin-stimulating agent affected hemoglobin levels in patients on peritoneal dialysis. Data were extracted from the Australian Renal Anaemia Management database for the years 2002 and 2008. Less frequent dosing and
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The American journal of clinical nutrition, 98(1), 65-81 (2013-05-31)
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Aurélie A Righetti et al.
The American journal of clinical nutrition, 97(6), 1364-1374 (2013-04-26)
Iron deficiency (ID) is a major cause of anemia, along with other nutritional, parasitic, and genetic factors. Accurate biomarkers are needed to estimate the relative contribution of ID to anemia. Soluble transferrin receptor (sTfR) is thought to be unaffected by

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