Recombinant Full Length Human APOBEC3A protein, Flag-tagged
Cat.No. : | APOBEC3A-5726HFL |
Product Overview : | Recombinant Full Length Human APOBEC3A protein, fused with C-terminal Flag tag, was expressed in mamanlian cells. |
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Source : | Mamanlian cells |
Species : | Human |
Tag : | Flag |
Form : | 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol. |
Molecular Mass : | 23 kDa |
Purity : | > 80% as determined by SDS-PAGE and Coomassie blue staining |
Concentration : | >50 ug/mL as determined by microplate BCA method |
Shipping : | The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. |
Gene Name : | APOBEC3A apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3A [ Homo sapiens ] |
Official Symbol : | APOBEC3A |
Synonyms : | A3A; ARP3; PHRBN; bK150C2.1; phorbolin 1; phorbolin-1; probable DNA dC->dU-editing enzyme APOBEC-3A |
Gene ID : | 200315 |
mRNA Refseq : | NM_145699 |
Protein Refseq : | NP_663745 |
MIM : | 607109 |
UniProt ID : | P31941 |
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◆ Lysates | ||
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Related Gene
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (18)
Ask a questionYes, genetic variants and polymorphisms of the APOBEC3A gene have been identified. These variations can affect the protein's activity or expression levels, potentially influencing its role in antiviral defense and mutagenesis.
Yes, our APOBEC3A proteins can be used in Western Blot.
Although APOBEC3A is primarily recognized for its antiviral activities, recent studies suggest it may play additional roles. It has been implicated in DNA repair processes, regulation of immune responses, and potential contributions to autoimmune disorders.
Given the anti-viral activity of APOBEC3A, there is interest in developing inhibitors that can block its function to limit viral replication. However, the development of specific and potent inhibitors is complex due to the structural similarities and overlapping functions of other APOBEC3 proteins.
While dysregulation of APOBEC3A activity has been implicated in cancer development, there is currently limited evidence linking alterations or mutations in the APOBEC3A gene to specific genetic disorders or diseases.
Several cellular factors, such as APOBEC3B, have been shown to interact with APOBEC3A and regulate its activity. Additionally, post-translational modifications, such as phosphorylation, may also modulate its function.
Several viruses have evolved strategies to counteract or evade the antiviral activity of APOBEC3A. For example, human immunodeficiency virus type 1 (HIV-1) encodes the protein Vif, which targets APOBEC3A (and other APOBEC3 proteins) for degradation.
APOBEC3A-induced DNA mutations can have diverse outcomes. On one hand, they can inhibit viral replication by introducing hypermutations that lead to non-functional viral genomes. On the other hand, excessive APOBEC3A activity or dysregulated expression can contribute to genomic instability and promote cancer development.
APOBEC3A has been reported to interact with several cellular proteins involved in DNA repair, immune responses, and viral pathogenesis. These interactions contribute to the regulation of its activity, but the full extent and functional consequences of these interactions are still being explored.
Yes, APOBEC3A-induced hypermutation can accelerate the evolution of various viruses, particularly RNA viruses. By introducing errors in viral genomes during replication, APOBEC3A can drive the emergence of viral variants that can potentially escape host immune responses or develop drug resistance.
APOBEC3A expression can vary among different cell types and tissues. It is predominantly expressed in tissues exposed to viral infections, such as the gastrointestinal tract, reproductive organs, and lymphoid tissues.
APOBEC3A belongs to a family of seven APOBEC3 proteins in humans, including APOBEC3B, APOBEC3C, APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H. These proteins share similar structural features and exhibit overlapping antiviral functions.
The antiviral and mutagenic activities of APOBEC3A make it an attractive target for therapeutic interventions. However, due to its potential for causing DNA mutations and genomic instability, careful consideration is needed to balance the benefits and potential risks in therapeutic applications.
No, APOBEC3A is primarily known for its activity on DNA molecules. It catalyzes the deamination of cytosines in single-stranded DNA, which can lead to the generation of uracil and subsequent DNA mutations.
There is evidence suggesting that certain environmental factors, such as chronic viral infections or exposure to genotoxic agents like cigarette smoke, can stimulate APOBEC3A expression and activity. These factors may contribute to increased DNA damage and mutagenesis.
While direct targeting of APOBEC3A for cancer treatment is challenging due to its mutagenic properties, there are ongoing efforts to develop therapeutic approaches that modulate its expression or activity to balance its antiviral effects while minimizing genomic instability.
The increased expression and mutational activity of APOBEC3A in certain cancers have led to investigations into its potential diagnostic and prognostic value. However, further research is needed to establish its utility as a clinical marker.
Dysregulation of APOBEC3A has been implicated in cancer development, specifically in various types of malignancies, including breast, cervical, and head and neck cancers. Elevated APOBEC3A expression and activity have been associated with increased mutagenesis and tumor evolution.
Customer Reviews (4)
Write a reviewthe APOBEC3A protein has proven to be invaluable in protein electron microscopy structure analysis.
I must applaud the APOBEC3A protein for its outstanding performance in Western blotting experiments.
I highly recommend the APOBEC3A protein for a variety of experimental applications.
The remarkable quality and reliability of the APOBEC3A protein have significantly contributed to the success of my structural investigations.
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