Analytical Data
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Gene name
AFUA_2G12630
- Application
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Alternative Names
(Allergen Asp f 13)(allergen Asp f 15)
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Species
Neosartorya fumigata
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O60022
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Expression Region
20-152aa
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Molecular Weight
20.0 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
Related Products
Protein Description
AFUA_2G12630 is a gene identified in the filamentous fungus Aspergillus fumigatus, a significant human pathogen known for causing invasive aspergillosis, particularly in immunocompromised individuals. The protein encoded by this gene is suspected to play a role in the organism's adaptation to various environmental stresses, such as oxidative stress and nutrient limitation, which are critical for its survival and virulence. Studies have indicated that proteins similar to AFUA_2G12630 may be involved in important cellular processes, including metabolism and cellular signaling, which contribute to the pathogen's ability to thrive in hostile environments like the human body. Understanding the functional properties of AFUA_2G12630 could provide insights into its role in fungal biology and potentially reveal therapeutic targets for treating Aspergillus infections. Recent advances in recombinant protein technology allow for the expression and characterization of this protein, enabling researchers to delve deeper into its biochemical properties and interactions. This research is essential for developing new antifungal strategies and improving our understanding of the pathogenic mechanisms utilized by A. fumigatus, thereby addressing the growing concern of antifungal resistance and the need for innovative treatment options.
