Analytical Data
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Gene name
A143V,V207A
- Application
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Alternative Names
(Protease precursor)(pPR)
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Species
Human cytomegalovirus
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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
P16753
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Expression Region
1-256aa(A143V,V207A)
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Molecular Weight
34.0 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
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Protein Description
The study of recombinant proteins A143V and V207A has gained significance within the field of structural biology and biochemistry due to their implications in understanding protein stability and functionality. These specific mutations are often investigated in the context of various diseases, particularly neurodegenerative disorders, where protein misfolding and aggregation play crucial roles. By introducing these mutations into model proteins, researchers aim to elucidate the effects on folding pathways, thermodynamic stability, and interaction with other biomolecules. The A143V variant, for instance, has been studied for its impact on the conformational dynamics of proteins, potentially altering their biological activity and interaction networks. Similarly, V207A has been explored for its effects on oligomerization processes, which are critical in the formation of functional protein complexes. Understanding these mutations at a molecular level not only provides insights into the basic principles of protein behavior but also holds potential for therapeutic applications. Through techniques like X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, researchers can obtain detailed structural information that contributes to the design of targeted interventions to mitigate pathogenic effects stemming from protein misfolding. Overall, the investigation of A143V and V207A serves as a pivotal aspect of the broader research endeavor to decode the complexities of protein biology and its associations with human diseases.
