Analytical Data
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Gene name
ASPRV1
- Application
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Alternative Names
Skin-specific retroviral-like aspartic protease Short name: SASPase Short name: Skin aspartic protease TPA-inducible aspartic proteinase-like protein Short name: TAPS SASP
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Species
Human
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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
Q53RT3
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Expression Region
191-326aa
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Molecular Weight
19.9 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
ASPRV1, a recombinant protein derived from the Aspartate-Serine-Proline-Rich Viral protein family, has garnered significant attention in the fields of virology and molecular biology. This protein is believed to play a crucial role in viral pathogenesis and host interactions, making it an important target for understanding viral mechanisms and developing therapeutic strategies. Previous studies have suggested that ASPRV1 may be involved in modulating host immune responses, potentially influencing the efficacy of antiviral treatments. The structural and functional characterization of ASPRV1 is essential for elucidating its role in the viral life cycle and for developing vaccines or antiviral drugs. Researchers are employing various techniques, including molecular cloning, protein expression systems, and biochemical assays, to study ASPRV1’s properties and interactions with host proteins. Insights gained from these investigations could lead to breakthroughs in our understanding of viral infection processes and the design of novel therapeutic interventions. The ongoing research into ASPRV1 represents a promising frontier in infectious disease research, highlighting the need for continued exploration of viral proteins and their implications for human health.
