cytoglobin Lentiviral Activation Particles (h): sc-402949-LAC

Human CYGB encodes cytoglobin, a hexacoordinate globin expressed in multiple tissues that binds oxygen and nitric oxide and contributes to redox balance. Cytoglobin participates in cellular responses to hypoxia and oxidative stress by modulating reactive oxygen species handling and nitric oxide bioavailability, influencing mitochondrial function and stress-adaptive transcriptional programs. Altered CYGB expression has been reported in contexts of tissue remodeling and fibrosis, vascular dysfunction, and tumor biology, where cytoglobin has been linked to changes in cellular survival, metabolism, and extracellular matrix signaling. These properties make CYGB a useful target for dissecting oxygen-sensing, redox-regulated pathways, and stress responses in physiologically relevant cell models.

cytoglobin 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 CYGB upregulation across a broader range of human cell types.

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