CTH Lentiviral Activation Particles (m): sc-430767-LAC

Mouse Cth encodes cystathionine gamma-lyase (CTH), a key transsulfuration enzyme that converts cystathionine to cysteine, ammonia, and α-ketobutyrate, linking methionine metabolism to cellular thiol homeostasis. By controlling cysteine availability and contributing to endogenous hydrogen sulfide (H2S) production, CTH influences redox buffering, glutathione synthesis, mitochondrial function, and stress-response signaling. CTH activity intersects with oxidative stress pathways and inflammatory regulation, with reported relevance to metabolic dysregulation, vascular biology, and neurobiology in disease models. Modulating Cth expression is therefore useful for dissecting sulfur amino acid flux, ROS sensitivity, and H2S-dependent signaling mechanisms in mammalian cells.

CTH 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 Cth upregulation across a broader range of human cell types.

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