Analytical Data
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Gene name
APOBEC3A
- Application
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Alternative Names
Phorbolin-1
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Species
Human
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Source
Yeast
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P31941
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Expression Region
1-199aa
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Molecular Weight
24.5 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
APOBEC3A (A3A) is a member of the APOBEC3 family of cytidine deaminases, which play critical roles in the innate immune response against retroviruses and other pathogens. A3A is particularly known for its ability to edit viral genomes, thereby inhibiting viral replication. In recent years, research has focused on understanding the structure, function, and mechanisms of A3A in both antiviral defense and its involvement in genomic mutations linked to cancer. Mutations induced by A3A can contribute to the genomic instability seen in various cancers, driving tumorigenesis through the alteration of critical genes. Given these dual roles, A3A presents a compelling target for therapeutic interventions. Researchers have been investigating the expression patterns and regulatory mechanisms governing A3A, as well as its interactions with other cellular proteins and its potential as a biomarker for cancer diagnosis and prognosis. Furthermore, studies have employed recombinant A3A protein to explore its enzymatic activity and substrate specificity, contributing to the development of strategies to harness or inhibit its activity for therapeutic use. Understanding A3A's dual nature is essential for developing approaches to mitigate its oncogenic potential while leveraging its antiviral properties.
