Tropomyosin γ Lentiviral Activation Particles (m2): sc-425595-LAC-2

Mouse Tpm3 encodes tropomyosin γ, an actin-binding coiled-coil protein that polymerizes along filamentous actin to regulate thin filament stability, myosin access, and force generation in cytoskeletal and contractile structures. By defining actin filament identity and dynamics, TPM3 contributes to processes including cell shape control, adhesion, migration, and mechanotransduction, influencing actomyosin remodeling in muscle and non-muscle cells. Dysregulated TPM3 function or expression has been associated with cytoskeletal defects and myopathies, and TPM3 fusion events are implicated in oncogenic signaling contexts that alter actin-dependent behavior. Genetic perturbation of Tpm3 in mouse models supports mechanistic studies of actin–myosin regulation, sarcomere assembly, and cytoskeletal pathway interactions using CRISPR-based editing and functional phenotyping.

Tropomyosin γ Lentiviral Activation Particles (m2) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Tpm3 upregulation across a broader range of human cell types.

Tropomyosin γ Lentiviral Activation Particles (m2) 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 Tpm3 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Tropomyosin γ expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Tpm3 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.