Analytical Data
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Gene name
APOBEC3C
- Application
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Alternative Names
APOBEC1-like Phorbolin I
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NRW3
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Expression Region
1-190aa
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Molecular Weight
49.8 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
APOBEC3C (Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3C) is a member of the APOBEC family of cytidine deaminases, which play a crucial role in the innate immune defense against viral infections, particularly retroviruses. This enzyme exhibits the ability to edit RNA and DNA by converting cytosine to uracil, thereby inducing mutations that can inhibit viral replication. Research has revealed that APOBEC3C specifically targets the genomic RNA of HIV-1 and other retroviruses, thereby acting as a potent antiviral factor. Studies have demonstrated that the activity of APOBEC3C is modulated by various factors including its interaction with the viral proteins and cellular factors, which can enhance or inhibit its antiviral effects. Notably, some viruses have evolved mechanisms to counteract the action of APOBEC3C, highlighting the ongoing evolutionary arms race between host defense mechanisms and viral strategies. As such, understanding the structure, function, and regulation of APOBEC3C is critical for developing potential therapeutic strategies aimed at enhancing its antiviral activity or inhibiting viral countermeasures. The ongoing research into its restructured protein forms aims to elucidate its mechanism of action in greater detail and potentially exploit this knowledge for therapeutic purposes, making APOBEC3C a significant focus in virology and immunology studies.
