Analytical Data
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Gene name
asa1
- Application
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Alternative Names
(Hemolysin)
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Species
Aeromonas sobria
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q06304
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Expression Region
25-443aa
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Molecular Weight
54.2 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
Asa1, a protein derived from the fungus Aspergillus, has drawn significant attention in recent years due to its potential applications in various biotechnological fields. The research on Asa1 recombinant protein focuses on exploring its unique structural and functional properties, particularly in relation to its enzymatic activities and stability under diverse environmental conditions. Given the increasing demand for sustainable and efficient biocatalysts in industrial processes, Asa1 is being investigated for its ability to facilitate bioconversion reactions, contributing to the production of biofuels, biodegradable materials, and pharmaceuticals. Additionally, understanding the molecular mechanisms of Asa1's action may lead to advancements in enzyme engineering, helping optimize its performance for specific applications. Researchers are utilizing advanced genetic engineering techniques to produce Asa1 in heterologous systems, ensuring a high yield and functional activity of the recombinant protein. As the global focus shifts towards greener technologies, Asa1's role in enabling eco-friendly practices and its potential in biotechnology make it a promising candidate for future research and commercial use. Moreover, studying Asa1 can also provide insights into the evolutionary biology of fungal proteins, as its functional characteristics may reveal adaptations to unique ecological niches. Overall, the exploration of Asa1 recombinant protein offers a multidisciplinary approach that bridges microbiology, bioengineering, and environmental science, paving the way for innovative solutions to contemporary challenges in sustainability and resource management.
