Analytical Data
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Gene name
FTH
- Application
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Alternative Names
FTH；FTH；FTHL6；Ferritin heavy chain
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P02794
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Expression Region
2-183aa
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AA Sequence
TTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNES
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Molecular Weight
48.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
FTH (Ferritin Heavy Chain) recombinant protein research has gained significant attention due to its crucial role in iron metabolism and cellular homeostasis. Ferritin is a multimeric protein complex that stores iron in a bioavailable form and releases it in a controlled manner, thus preventing iron-induced oxidative stress. The heavy chain of ferritin is primarily responsible for ferroxidase activity, facilitating the oxidation of ferrous iron to ferric iron, which is then sequestered within the protein's shell. Enhanced understanding of FTH through recombinant DNA technology has paved the way for producing high quantities of functional protein for various applications in biomedical research, including drug delivery, iron supplementation therapies, and imaging techniques. Additionally, FTH's role in modulating immune responses and its potential as a biomarker for certain diseases underscore its relevance in clinical diagnostics and therapeutic strategies. Considering the rising prevalence of iron-related disorders and the importance of maintaining iron homeostasis in health and disease, researching FTH recombinant protein holds great promise for generating innovative solutions in the fields of medicine and biotechnology.
