Analytical Data
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Gene name
fim3
- Application
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Alternative Names
fim3；Fimbrin-3
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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
P17835
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Expression Region
26-204aa
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AA Sequence
NDGTIVITGSISDQTCVIEEPSTLNHIKVVQLPKISKNALRNDGDTAGATPFDIKLKECPQALGALKLYFEPGITTNYDTGDLIAYKQTYNASGNGNLSTVSSATKAKGVEFRLANLNGQHIRMGTDKTTQAAQTFTGKVTNGSKSYTLRYLASYVKKPKEDVDAAQITSYVGFSVVYP
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Molecular Weight
21.2 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
FIM3, or Ferritin-like Protein 3, is a significant component in various biochemical processes, particularly in iron metabolism and homeostasis within living organisms. Research on FIM3 has gained momentum due to its potential implications in both health and disease. Scientists have been particularly interested in understanding its structure and function because FIM3 can influence iron storage and regulate oxidative stress within cells. Abnormal FIM3 levels have been linked to several pathologies, including neurodegenerative diseases, infections, and cancer. As a member of the ferritin superfamily, FIM3 shares similarities with traditional ferritin proteins, yet it possesses unique characteristics that suggest it may play specific roles in different biological contexts. Recent advancements in recombinant DNA technology have facilitated the production of FIM3 recombinant proteins, enabling detailed studies of their biochemical properties and interactions. This research not only aims to elucidate the mechanistic aspects of FIM3 in iron metabolism and cellular responses to oxidative stress but also explores its potential as a therapeutic target or biomarker for various diseases. Understanding FIM3's functional dynamics through recombinant protein studies could lead to novel interventions in iron-related disorders and enhance our general knowledge of protein functions in biological systems. Overall, the study of FIM3 recombinant proteins represents a promising frontier in biochemistry and medicine, with implications for improving health outcomes and developing new therapeutic strategies.
