Analytical Data
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Gene name
fis
- Application
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Alternative Names
fis；TTC11；Mitochondrial fission 1 Protein
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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
P0A6R7
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Expression Region
1-98aa
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AA Sequence
MFEQRVNSDVLTVSTVNSQDQVTQKPLRDSVKQALKNYFAQLNGQDVNDLYELVLAEVEQPLLDMVMQYTRGNQTRAALMMGINRGTLRKKLKKYGMN
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Molecular Weight
12.7 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
FIS (Fifty-five kilodalton Inner membrane protein of S. cerevisiae) is a critical protein involved in various cellular processes in yeast, particularly in ribosome biogenesis and mitochondrial function. Research into FIS has gained momentum due to its potential role in understanding fundamental cellular mechanisms and its implications in disease contexts. The study of FIS is particularly relevant in the field of cell biology, where it is investigated as a model to elucidate the dynamics of protein interactions and cellular responses to stress. Its involvement in mitochondrial activities links it to metabolic disorders and aging, making it a significant target for studies aiming to uncover the underlying mechanisms of these conditions. Advances in recombinant protein technology have enabled the generation of purified FIS for detailed structural and functional analyses, enhancing our understanding of its biological significance. Furthermore, the exploration of FIS interactions with other cellular components may reveal novel pathways and therapeutic targets, paving the way for innovations in biotechnology and medicine. Overall, FIS serves as a vital indicator of cellular health and function, representing a focal point for ongoing research in cellular biology and related disciplines.
