Analytical Data
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Gene name
FER1L3
- Application
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Alternative Names
Fer 1 like 3. myoferlin (C. elegans) ; Fer 1 like family member 3; Fer 1 like protein 3; Fer-1-like protein 3; FER1L3; myoF; MYOF_HUMAN; Myoferlin
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NZM1
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Expression Region
655-754aa
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AA Sequence
DAVNTLLAMAERLQTNIEALKSGIQGKIPANQLAELWLKLIDEVIEDTRYTLPLTEGKANVTVLDTQIRKLRSRSLSQIHEAAVRMRSEATDVKSTLAEI
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Molecular Weight
36.74 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
FER1L3, or Ferritin Family Member 1-Like 3, is a protein that has garnered attention in molecular biology due to its potential role in cellular processes and disease mechanisms. Research indicates that FER1L3 may be involved in regulating iron metabolism and oxidative stress, which are critical factors in various physiological and pathological conditions. Its expression patterns have been linked to several diseases, including neurodegenerative disorders and cancer, suggesting that it could be a significant player in disease progression and response to therapy. Furthermore, studies have shown that FER1L3 interacts with other proteins and cellular pathways, highlighting its potential as a biomarker for disease and a target for therapeutic intervention. As scientists continue to explore the structure and function of FER1L3, the development of recombinant protein technologies has facilitated the investigation of its biological activities and interactions. This research could pave the way for novel insights into iron-related diseases and contribute to the development of innovative treatments. Understanding the biochemical properties and cellular roles of FER1L3 is crucial for unveiling its full therapeutic potential and could lead to breakthroughs in managing diseases linked to iron dysregulation.
