S-100A5 Lentiviral Activation Particles (h): sc-418401-LAC

Human S100A5 encodes S-100A5, a Ca2+-binding EF-hand protein in the S100 family that acts as a calcium sensor to modulate protein–protein interactions and cell state–dependent signaling. S-100A5 is linked to calcium-regulated processes including cytoskeletal organization, membrane dynamics, and transcriptional responses, consistent with broader S100 protein involvement in neuronal and epithelial biology. Altered S100 family expression patterns have been associated with inflammation-related signaling and cancer-relevant pathways such as MAPK and NF-κB, making S100A5 a useful marker and mechanistic node for studies of cellular stress responses and differentiation programs. Its context-dependent expression supports applications in investigating lineage specification, signal integration, and pathway rewiring in disease-relevant models.

S-100A5 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 S100A5 upregulation across a broader range of human cell types.

S-100A5 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 S100A5 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous S-100A5 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native S100A5 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.