APOBEC3A Lentiviral Activation Particles (h): sc-418267-LAC

Human APOBEC3A (apolipoprotein B mRNA editing enzyme catalytic subunit 3A) is a cytidine deaminase that catalyzes C-to-U editing in single-stranded DNA and RNA, contributing to intrinsic immunity by restricting viral replication and limiting retroelement activity. By acting on exposed ssDNA during replication stress and DNA repair, APOBEC3A intersects with genome maintenance pathways and can increase mutational burden when dysregulated. Aberrant APOBEC3A activity has been linked to characteristic mutation signatures observed in multiple tumor types and is studied in the context of inflammation-associated genomic instability. Researchers use APOBEC3A as a model to interrogate antiviral restriction, DNA damage responses, and mechanisms shaping somatic mutagenesis.

APOBEC3A Lentiviral Activation Particles (h) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient APOBEC3A upregulation across a broader range of human cell types.

APOBEC3A Lentiviral Activation Particles (h) deliver all functional components of the synergistic activation mediator (SAM) system via lentiviral transduction. The system comprises three particle preparations co-transduced into target cells: one encoding catalytically inactive dCas9 (D10A and N863A mutations) fused to the VP64 transactivation domain with a blasticidin resistance gene; one encoding the MS2-p65-HSF1 fusion protein with a hygromycin resistance gene; and one encoding a target-specific 20 nt sgRNA fused to two MS2 RNA aptamers with a puromycin resistance gene. Following lentiviral transduction and genomic integration of the expression cassettes, the SAM components are stably expressed and assemble at the target locus within the proximal promoter region upstream of the APOBEC3A transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous APOBEC3A expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native APOBEC3A genomic locus and regulatory architecture.

The lentiviral format offers several practical advantages: stable genomic integration supports heritable activation across cell divisions; high-titer particle preparations eliminate the need for in-house viral production; and compatibility with primary, non-dividing, and transfection-resistant cell types expands experimental accessibility. Successful transduction can be confirmed and enriched through triple antibiotic selection using puromycin, hygromycin, and blasticidin.

For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.