HIF PHD3 Lentiviral Activation Particles (m): sc-431083-LAC

Egln3 encodes hypoxia-inducible factor prolyl hydroxylase 3 (HIF PHD3), an oxygen-sensing dioxygenase that hydroxylates HIF-α subunits to promote VHL-dependent ubiquitination and proteasomal degradation under normoxia. Through regulation of HIF transcriptional programs, HIF PHD3 helps coordinate cellular responses involving angiogenic signaling, glycolytic metabolism, mitochondrial function, redox balance, and adaptation to low-oxygen microenvironments. In mouse systems, altered Egln3 activity is widely used to interrogate hypoxia pathway dynamics across development and tissue remodeling, where oxygen availability shapes cell fate and stress responses. Dysregulation of HIF–PHD signaling is frequently leveraged as a mechanistic framework in models of ischemia, inflammation, fibrosis, and tumor biology, supporting Egln3 as a key node for pathway-focused research.

HIF PHD3 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 Egln3 upregulation across a broader range of human cell types.

HIF PHD3 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 Egln3 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous HIF PHD3 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Egln3 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.