Analytical Data
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Gene name
FTL
- Application
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Alternative Names
FTL;Ferritin light 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
P02792
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Expression Region
2-175aa
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AA Sequence
SSQIRQNYSTDVEAAVNSLVNLYLQASYTYLSLGFYFDRDDVALEGVSHFFRELAEEKREGYERLLKMQNQRGGRALFQDIKKPAEDEWGKTPDAMKAAMALEKKLNQALLDLHALGSARTDPHLCDFLETHFLDEEVKLIKKMGDHLTNLHRLGGPEAGLGEYLFERLTLKHD
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Molecular Weight
24.0 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
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Protein Description
FTL (Ferritin Light Chain) is a subunit of ferritin, a crucial protein involved in iron storage and homeostasis in cells. The study of FTL is significant due to its essential role in cellular iron metabolism and the prevention of oxidative stress. Dysregulation of ferritin and its subunits, including FTL, has been implicated in various pathological conditions, including neurodegenerative diseases, cancer, and inflammatory disorders. Research has shown that FTL can participate in the formation of reactive oxygen species when iron metabolism is disturbed, underscoring its potential as a biomarker and therapeutic target. Additionally, FTL plays a role in the immune response and may influence cellular processes such as proliferation and apoptosis. Given the increasing prevalence of iron-related diseases and the challenges associated with current treatment modalities, understanding the structure, function, and regulatory mechanisms of FTL has gained substantial attention. Recent advances in molecular biology and biochemistry have enabled researchers to explore FTL's interactions with other cellular components and its potential applications in drug development and disease management. As a result, ongoing research on FTL and its reorganization could lead to novel insights into both basic biological processes and clinical interventions, making it a vital area of exploration in biomedical research.
