Analytical Data
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Gene name
Ferritin light chain/FTL
- Application
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Alternative Names
Ferritin Light Chain; Ferritin Light Polypeptide-Like 3; L Apoferritin; Ferritin L Subunit
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Species
Horse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P02791
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Expression Region
Met1~Asp175
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Molecular Weight
24kDa
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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
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Protein Description
Ferritin light chain (FTL) is a crucial protein involved in iron storage and homeostasis within cells. It forms part of the ferritin complex, which plays a vital role in maintaining cellular iron levels and protecting cells from iron-induced oxidative stress. Abnormal levels of FTL have been associated with various diseases, including neurodegenerative disorders, cancer, and cardiovascular diseases, highlighting its potential as a biomarker and therapeutic target. The study of recombinant FTL proteins has gained traction due to their importance in understanding iron metabolism and their applications in biotechnology and medicine. By producing FTL through recombinant DNA technology, researchers can obtain large quantities of pure protein for biochemical studies, structural analysis, and functional assays. This enables a deeper investigation into the mechanisms of iron storage and release, as well as the role of FTL in pathophysiological conditions. Furthermore, recombinant FTL proteins can facilitate the development of new diagnostic tools and therapeutic strategies, underscoring the significance of ongoing research in this area. The exploration of FTL's structure-function relationship and its interactions with other cellular molecules continues to be a promising field for elucidating the complexities of iron metabolism and its broader implications for health and disease.
