CYP4X1 Lentiviral Activation Particles (m): sc-429886-LAC

Cyp4x1 encodes the cytochrome P450 enzyme CYP4X1, a membrane-associated monooxygenase implicated in fatty acid and eicosanoid metabolism, including oxidation of arachidonic acid–derived lipids that can modulate inflammatory signaling and vascular or neuronal homeostasis. As part of the broader P450 oxidative pathway, CYP4X1 activity influences cellular redox balance and lipid mediator availability, linking it to processes such as oxidative stress responses and intercellular communication. In mouse tissues, Cyp4x1 expression has been reported in brain-enriched contexts, supporting research into lipid signaling networks relevant to neuroinflammation and neurovascular regulation. Altered regulation of P450 lipid-metabolizing enzymes is frequently examined in models of metabolic and inflammatory disorders, making Cyp4x1 a useful node for pathway-focused mechanistic studies.

CYP4X1 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 Cyp4x1 upregulation across a broader range of human cell types.

CYP4X1 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 Cyp4x1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous CYP4X1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Cyp4x1 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.