Analytical Data
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Gene name
ASP2
- Application
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Alternative Names
(Secreted protein ASP-2)
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Species
Necator americanus
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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
Q7Z1H1
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Expression Region
20-210aa
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Molecular Weight
26.7 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
The ASP2 protein, a member of the aspartic protease family, has garnered significant interest in biomedical research due to its potential implications in various physiological and pathological processes. Originally identified in fungi, ASP2 is believed to play a critical role in protein degradation, metabolism, and cellular signaling. Its importance is underscored by its involvement in diseases where dysregulated proteolytic activity can lead to inflammation, cancer progression, and neurodegenerative disorders. Recent studies have aimed to understand the structural and functional properties of ASP2 through recombinant protein techniques, allowing for the production of purified ASP2 variants for detailed biochemical characterization. This research not only enhances our understanding of ASP2's enzymatic mechanisms but also provides insights into its substrate specificity and potential as a therapeutic target. By elucidating the functional aspects of ASP2, researchers hope to develop novel interventions for diseases associated with aberrant protease activity, making it a promising candidate in the field of drug discovery and development. Overall, the study of ASP2 recombinant protein represents a significant step towards harnessing its biological potential for therapeutic applications.
