LTRPC7 Lentiviral Activation Particles (h): sc-402820-LAC

TRPM7 (LTRPC7) encodes a unique channel-kinase that conducts divalent cations, particularly Mg²⁺ and Ca²⁺, while coupling ion flux to a cytosolic serine/threonine kinase domain. By regulating intracellular magnesium homeostasis, cytoskeletal dynamics, and Ca²⁺-dependent signaling, TRPM7 influences processes including cell proliferation, migration, mechanotransduction, and cellular stress responses. TRPM7 activity interfaces with pathways linked to membrane excitability and kinase-mediated signaling networks that shape inflammatory signaling and metabolic adaptation. Dysregulated TRPM7 expression or function has been associated with neurological injury and neurodegeneration, cardiovascular remodeling, and altered growth behavior in multiple cancer contexts, making it a relevant node for pathway-centric functional genomics studies.

LTRPC7 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 TRPM7 upregulation across a broader range of human cell types.

LTRPC7 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 TRPM7 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous LTRPC7 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native TRPM7 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.