Analytical Data
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Gene name
FTL3
- Application
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Species
Glycine max
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
E3NYP3
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Expression Region
1-176aa
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Molecular Weight
25.7 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
FTL3 is a recombinant protein that plays a crucial role in various biological processes, particularly in the regulation of iron metabolism and storage within cells. As an isoform of ferritin, the protein is part of the larger ferritin family that serves to sequester and release iron in a controlled manner, thereby preventing iron-mediated oxidative damage. Research into FTL3 is particularly significant due to its implications in several diseases, including neurodegenerative disorders and cancer, where dysregulation of iron homeostasis has been implicated. Recent advancements in recombinant DNA technology have facilitated the production of FTL3 in various expression systems, allowing for detailed studies of its structure-function relationships, interactions with other biomolecules, and role in iron metabolism under both physiological and pathological conditions. Investigating FTL3 not only enhances our understanding of iron biology but also opens avenues for developing novel therapeutic strategies targeting iron-related diseases. Overall, the study of FTL3 as a recombinant protein offers valuable insights into iron regulation and its broader implications for health and disease.
