Analytical Data
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Gene name
APOBEC3G
- Application
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Alternative Names
(APOBEC-related cytidine deaminase, APOBEC-related protein, ARCD)(APOBEC-related protein 9, ARP-9)(CEM-15, CEM15)
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9HC16
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Expression Region
1-384aa
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Molecular Weight
62.4 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
APOBEC3G is a crucial member of the APOBEC3 family of cytidine deaminases, which play a vital role in the innate immune response against retroviruses, including HIV. Initially identified for its ability to inhibit viral replication by deaminating cytidine residues in viral RNA, resulting in hypermutation and ultimately preventing the production of infectious viral particles, APOBEC3G has garnered significant research interest. However, HIV has developed sophisticated mechanisms to counteract this defense, including the viral protein Vif, which degrades APOBEC3G, undermining its antiviral effects. Understanding the structure and function of APOBEC3G, along with its interactions with viral proteins, is essential for unraveling its precise role in immune defense and retroviral pathogenesis. This knowledge could pave the way for novel therapeutic strategies aimed at enhancing the antiviral activity of APOBEC3G or inhibiting the viral countermeasures, thereby improving outcomes in HIV-infected individuals. Researchers are increasingly focused on dissecting the biochemical properties of APOBEC3G, exploring its potential roles beyond retroviral defense, and investigating its implications in other diseases, including cancer, where its mutagenic activity can influence tumor progression. The ongoing study of APOBEC3G and related proteins continues to shed light on their complex functionalities and potential as targets in viral therapy and cancer treatment.
