Analytical Data
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Gene name
FTL3
- Application
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Alternative Names
FTL3；FTL3；Protein RICE FLOWERING LOCUS T 1
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Species
E.coli
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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
Q8VWH2
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Expression Region
1-178aa
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AA Sequence
MAGSGRDDPLVVGRIVGDVLDPFVRITNLSVSYGARIVSNGCELKPSMVTQQPRVVVGGNDMRTFYTLVMVDPDAPSPSNPNLREYLHWLVTDIPGTTGATFGQEVMCYESPRPTMGIHRLVFVLFQQLGRQTVYAPGWRQNFSTRNFAELYNLGSPVATVYFNCQREAGSGGRRVYP
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Molecular Weight
19.7 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, or ferritin-like protein 3, is a member of the ferritin family, which plays a crucial role in iron storage and homeostasis within biological systems. This protein has garnered attention due to its potential involvement in various physiological and pathological processes, including oxidative stress response, inflammation, and cellular iron metabolism. Research has shown that FTL3 may have unique functions distinct from other ferritins, possibly influencing neurological health and disease. For instance, studies suggest that altered expression of FTL3 is associated with neurodegenerative disorders, raising questions about its role in neuronal survival and function. The reconstitution and structural analysis of FTL3 at the molecular level are essential for understanding its biochemical properties and interactions with iron. Furthermore, exploring FTL3's regulatory mechanisms and its interactions with other cellular pathways could provide insights into its therapeutic potential. As research progresses, FTL3 may emerge as a significant biomarker or therapeutic target, highlighting the need for comprehensive studies on its functional roles and implications in health and disease. Thus, the investigation of FTL3 and its recombinant forms is critical for advancing our understanding of iron metabolism and its broader impacts on human health.
