TRPM8 Lentiviral Activation Particles (h): sc-401744-LAC

TRPM8 (transient receptor potential cation channel subfamily M member 8) encodes a cold- and menthol-sensitive, Ca2+-permeable ion channel that functions as a key detector of environmental cooling and chemical agonists in sensory neurons and other cell types. TRPM8 activity regulates membrane excitability and intracellular calcium signaling, influencing downstream processes such as kinase signaling, transcriptional responses, and neurogenic inflammation pathways. In addition to roles in somatosensation, TRPM8 has been linked to epithelial and neuronal physiology and is frequently studied in the context of pain signaling, peripheral neuropathy mechanisms, and altered calcium homeostasis. Dysregulated TRPM8 expression or channel activity has been reported in multiple disease-relevant settings, supporting its use as a molecular entry point for mechanistic studies of sensory transduction and Ca2+-dependent signaling networks.

TRPM8 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 TRPM8 upregulation across a broader range of human cell types.

TRPM8 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 TRPM8 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous TRPM8 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native TRPM8 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.