Analytical Data
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Gene name
Stfa2
- Application
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Alternative Names
Stfa2；Stf-2；Stf2；Stefin-2
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Species
Mouse
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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
P35174
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Expression Region
1-103aa
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AA Sequence
MTEYTRKIKGGLSEARPATSEIQEIADKVRPLLEEKTNEKYEKFKAIEYKVQVVQGLNYFIKMNVGRGCYLHINVLSGISSENDLELTGYQTNKAKNDELTYF
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Molecular Weight
17.1 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
Stfa2 is a recombinant protein that has garnered significant attention in the field of biotechnology and molecular biology due to its potential applications in various biotherapeutic processes. Initially identified as a part of the antifungal defense system in certain organisms, Stfa2 has shown promise in its ability to inhibit the growth of pathogenic fungi, making it a key candidate for developing novel antifungal agents. Researchers have focused on elucidating its structure and function, aiming to understand the molecular mechanisms underlying its antifungal activity. The recombinant expression of Stfa2 in suitable host systems allows for functional studies and the exploration of its interactions with fungal cells. This research is crucial as fungal infections pose a serious health threat, particularly for immunocompromised individuals. By harnessing the properties of Stfa2, scientists hope to contribute to the development of more effective treatments for fungal infections, addressing a pressing need in the field of medicine. Additionally, understanding the pathways by which Stfa2 exerts its effects can pave the way for innovative strategies in pathogen control and provide insights into protein engineering for therapeutic uses. The ongoing investigation into Stfa2 is not only expanding our knowledge of antifungal proteins but is also offering avenues for biotechnological advancements in the treatment of fungal diseases.
