Phorbolin 1 _ APOBEC3A
- Known as:
- Phorbolin 1 _ APOBEC3A
- Catalog number:
- Y213881
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- Phorbolin 1 _ APOBEC3A
Related genes to: Phorbolin 1 _ APOBEC3A
- Gene:
- APOBEC3A NIH gene
- Name:
- apolipoprotein B mRNA editing enzyme catalytic subunit 3A
- Previous symbol:
- -
- Synonyms:
- ARP3, PHRBN
- Chromosome:
- 22q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-12-12
- Date modifiied:
- 2016-10-05
Related products to: Phorbolin 1 _ APOBEC3A
Related articles to: Phorbolin 1 _ APOBEC3A
- : Bisulfite-based cell-free DNA (cfDNA) methylation assays enable the detection of clinically valuable epigenetic biomarkers but often cause DNA degradation and inconsistent conversion efficiency, limiting performance in low-input liquid biopsy samples. We aimed to develop and evaluate a fully enzymatic cfDNA methylation workflow that preserves DNA integrity and supports quantitative clinical detection. : The assay integrates TET2-mediated oxidation and APOBEC3A deamination with RNase H2-guided primer design, uracil-DNA glycosylase error suppression, and dual-probe detection compatible with quantitative PCR (qPCR) and digital PCR (dPCR). Performance was assessed using serial dilutions of methylated HT29 DNA, unmethylated controls, and plasma cfDNA from colorectal cancer (CRC) patients and healthy donors. Analytical sensitivity, linearity, and concordance between platforms were evaluated. : The 40-marker panel demonstrated higher cumulative methylation scores and more frequent methylation-positive signals in CRC cfDNA compared to controls. dPCR confirmed single-molecule resolution and clear discrimination between methylated and unmethylated templates, with occasional double-positive partitions consistent with mixed allelic methylation. Signal intensity across the dilution series followed a four-parameter logistic model, achieving detection sensitivity below 0.2% methylated DNA. qPCR and dPCR results showed strong correlation across the HT29 dilution series (R = 0.80) and high concordance in classifying CRC and healthy samples. : This TET2-APOBEC-based enzymatic cfDNA assay enables sensitive, quantitative, sequencing-free methylation detection under gentle conditions, supporting its application in early colorectal cancer screening and routine clinical liquid biopsy workflows. - Source: PubMed
Publication date: 2026/05/18
Aguilera-Diaz AlmudenaFeinberg Philip BHuang JianminSpier EugeneBarany FrancisBacolod Manny D - Biological sex is a key modifier of HIV pathogenesis, with women more frequently achieving spontaneous viral control than men. Toll-like receptor 7 (TLR7), an endosomal RNA sensor encoded on the X chromosome that escapes X-inactivation, plays a pivotal role in antiviral immunity and is increasingly targeted in HIV cure strategies aimed at reversing viral latency. However, it remains unclear whether TLR7-driven immune responses differ by sex in the context of HIV infection. - Source: PubMed
Publication date: 2026/04/21
Huber AlisaVadaq NadiraGroenendijk Albert LRios-Vazquez VictoriaRuijten Suzanne D EKnoll RainerMartens Joost A HNavas AdrianaMatzaraki VasilikiVos Wilhelm A J WBlaauw Marc J Tvan Eekeren Louise EJacobs-Cleophas Maartje C PAschenbrenner Anna CSchultze Joachim Lvan Lunzen JanNetea Mihai Gvan der Ven Andre J A MJoosten Leo A BDos Santos Jéssica C - Precise enzymatic assays for cytidine deaminases (CDAs), which catalyze the deamination of cytidine (C) and 5-methylcytidine (5mC) into uridine (U) and thymidine (T), are essential tools in both epigenetics and genome editing. However, current biochemical methods have been hindered by cumbersome procedures and the challenge of concurrently assessing C and 5mC deamination. To address these limitations, we developed a novel Argonaute-based deaminase detection (ABDD) assay. This method employs guide-DNA-directed hyperthermophilic Argonaute (Ago) to selectively cleave the fluorescence-labeled deamination products at U and T positions, respectively, enabling quantification of both C and 5mC deamination within 30 min by direct visualization of urea-PAGE. The ABDD assay was validated using APOBEC3A, APOBEC3H, and gain-of-function mutants A3H-RL18AA and A3A-Y130F, demonstrating concentration-dependent activity. The kinetic parameters and for A3H are 8.6 × 10 s and 4.7 μM, respectively, which align well with those from conventional glycosylase-based assays. ABDD also proved to be robust over a broad pH range of 5.5 to 8.5 and enabled accurate measurement in complex cellular lysates. In summary, the ABDD assay establishes a versatile and efficient platform for the functional and kinetic analysis of CDAs, offering a powerful tool with broad applicability in related research fields. - Source: PubMed
Publication date: 2026/05/04
Xu HeshanXu ShuaiLi MengyuZhang YiwenXu XiaoyiGuo XiangLiu QianFeng Yan - DNA-editing enzymes such as those in the APOBEC family of cytidine deaminases play important roles in both normal and pathogenic function, while engineered enzymes offer exciting new possibilities for genome editing. Despite their importance, widely used assays for DNA-editing enzymes are time-consuming and expensive. Here, we describe a new assay for DNA-editing enzymes in which the substrate in the reaction is a chemiluminescent deoxyribozyme called Supernova. Editing alters the sequence of Supernova, which results in a change in catalytic activity and light production. By analyzing a data set of Supernova variants previously identified by selection and high-throughput sequencing, it was possible to generate sensors with a wide range of specificities. Sensors were also developed for APOBEC3A, a cytidine deaminase which converts C to U in single-stranded DNA and RNA. These include a turn-off sensor that produces light 14-fold slower after incubation with recombinant APOBEC3A than in its absence, and a turn-on sensor that generates light 10-fold faster after incubation with APOBEC3A than in its absence. Assays that use these sensors are faster and less expensive than existing ones, and should be particularly useful for applications such as high-throughput screening. - Source: PubMed
Publication date: 2026/04/24
Jakubec MartinSvoboda MichalKurfürst JaroslavSvehlova KaterinaVeverka VáclavCurtis Edward A - APOBEC-mediated cytidine deamination is a major endogenous source of mutagenesis in human cancers and has been linked to tumor evolution, clonal diversification and therapeutic resistance. Among the APOBEC family, APOBEC3A (A3A) is a potent and inducible cytidine deaminase, with dynamic and context-dependent activation. Most approaches for studying the role of A3A in cancer infer A3A activity indirectly via its expression level or retrospective mutational signatures, or through molecular assays that are limited to endpoint measurements and do not readily allow longitudinal interrogation of A3A editing dynamics. Therefore, quantifying the timing, persistence, and cellular heterogeneity of A3A activity remains challenging. Here, we describe ApoFLARE, a genetically encoded reporter that converts A3A-mediated cytidine deamination into a quantitative luminescent signal in living cells. ApoFLARE allows for scalable, ratiometric measurement of editing activity and enables time-resolved analysis of editing kinetics. Reporter activation is selectively dependent on A3A catalytic function and was absent in A3A-deficient, but not A3B-deficient cells. Under stress and targeted therapy conditions, reporter activity correlated with endogenous RNA editing measured by digital droplet PCR, including contexts in which catalytic activity persisted beyond transient A3A transcript induction. Thus, ApoFLARE offers a scalable platform to investigate the regulation, kinetics, and heterogeneity of A3A editing. - Source: PubMed
Publication date: 2026/03/14
Di Marco Maria VittoriaButler Braeden LEggers Christopher THata Aaron N