hDcp2 Lentiviral Activation Particles (h): sc-418511-LAC

DCP2 encodes the human mRNA decapping enzyme hDcp2, a core component of cytoplasmic mRNA turnover that removes the 5′ cap structure to initiate 5′→3′ decay. Through its function in the decapping complex with cofactors such as DCP1 and decapping activators, hDcp2 contributes to RNA quality control, processing body (P-body) dynamics, and transcriptome remodeling downstream of stress responses and signaling-dependent changes in gene expression. DCP2-regulated decay interfaces with pathways controlling translation, RNA surveillance, and cellular adaptation to environmental cues, making it relevant to studies of post-transcriptional regulation. Altered mRNA decapping and dysregulated RNA stability have been linked to disease-associated gene expression programs, supporting investigation of DCP2 in models of oncogenic signaling, neurobiology, and host–pathogen interactions.

hDcp2 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 DCP2 upregulation across a broader range of human cell types.

hDcp2 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 DCP2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous hDcp2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native DCP2 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.