F6754
Ferritin from human liver
Type IV, 10 μg/mL
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R$ 2.608,00
About This Item
Produtos recomendados
fonte biológica
human liver
Nível de qualidade
esterilidade
0.2 μm filtered
tipo
Type IV
Ensaio
≥95% (SDS-GE)
Formulário
liquid
peso molecular
H subunit ~21 kDa
L subunit ~19 kDa
~440 kDa (a shell of 24 protein subunits (apoferritin) and a core of Fe3+ ions)
embalagem
vial of 2 μg
concentração
10 μg/mL
temperatura de armazenamento
2-8°C
Informações sobre genes
human ... FTH1(2495) , FTL(2512) , FTMT(94033)
Descrição geral
Ferritin comprises 24-subunit and belongs to the ferritin-like diiron-carboxylate protein superfamily.[1] Ferritin exists as heavy (H) and light (L) subunits. Liver ferritin is majorly L subunit and the spleen has the H submit.[2] The L subunit is mapped to human chromosome 9q13.33[3] and the H subunit 11q12.3.[4]
Aplicação
Ferritin from human liver has been used as model protein in size-exclusion high-performance liquid chromatography technique and for synthetic nanopore translocation studies.[5] It has also been used to test its effect on the susceptibility of shrimp (Litopenaeus vannamei) to the white spot syndrome virus.[1]
Ações bioquímicas/fisiológicas
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.[1] The abnormal levels of ferritin are correlated to many tumors associated with the prostate, breast and brain.[6] High levels of ferritin are implicated in inflammation[6] and macrophage activation syndrome (MAS).[7] Mutations in the light subunit chain can lead to the neurodegenerative disease, hereditary ferritinopathy.[3]
forma física
Solution in 10 mM Tris, 150 mM NaCl, pH 8.0, and 0.1% sodium azide.
Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
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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
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
Erik R Anderson et al.
Comprehensive Physiology, 3(1), 315-330 (2013-05-31)
Iron is an essential nutrient that is tightly regulated. A principal function of the liver is the regulation of iron homeostasis. The liver senses changes in systemic iron requirements and can regulate iron concentrations in a robust and rapid manner.
Alexander Michael Dohnal et al.
International journal of cancer, 119(12), 2870-2877 (2006-10-04)
The potential immunogenicity of acute lymphoblastic leukemia of the T cell (T-ALL), a small subgroup of childhood leukemia with increased risk for treatment failure and early relapse, was addressed by serological identification of leukemia-derived antigens by recombinant expression cloning (SEREX).
A novel FTL mutation responsible for neuroferritinopathy with asymmetric clinical features and brain anomalies.
Sébastien Moutton et al.
Parkinsonism & related disorders, 20(8), 935-937 (2014-06-08)
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