Metallothionein 2A Lentiviral Activation Particles (h): sc-410889-LAC

MT2A encodes metallothionein 2A, a cysteine-rich metal-binding protein that buffers intracellular zinc and copper and contributes to detoxification of toxic metals such as cadmium and mercury. By regulating metal ion homeostasis and redox balance, MT2A influences oxidative stress responses, mitochondrial function, and transcriptional programs mediated by metal-dependent factors. MT2A expression is responsive to inflammatory and stress signaling, including NRF2-driven antioxidant pathways, and can modulate apoptosis and cell survival under toxic or metabolic stress. Dysregulated MT2A activity and expression have been associated with cancer biology, metabolic and liver disorders, and neurodegenerative mechanisms where metal dyshomeostasis and oxidative damage are prominent.

Metallothionein 2A 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 MT2A upregulation across a broader range of human cell types.

Metallothionein 2A 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 MT2A transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Metallothionein 2A expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native MT2A 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.