CYPOR Lentiviral Activation Particles (m): sc-422345-LAC

Mouse Por encodes cytochrome P450 oxidoreductase (CYPOR), the obligate electron donor to microsomal cytochrome P450 enzymes that catalyze oxidative metabolism of xenobiotics, steroids, fatty acids, and retinoids. CYPOR transfers reducing equivalents from NADPH to CYPs, linking cellular redox balance to endoplasmic reticulum–associated detoxification and lipid homeostasis pathways. By governing CYP-dependent bioactivation and clearance reactions, Por influences oxidative stress responses and tissue-specific metabolic capacity in liver and extrahepatic organs. Dysregulated CYPOR activity is therefore relevant to studies of drug–drug interactions, endocrine and lipid signaling perturbations, and metabolic phenotypes associated with altered CYP function.

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

CYPOR Lentiviral Activation Particles (m) 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 Por transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous CYPOR expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Por 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.