EMMPRIN/CD147 Lentiviral Activation Particles (m): sc-419369-LAC

Basigin (Bsg), also known as EMMPRIN/CD147, is a transmembrane immunoglobulin superfamily glycoprotein that functions as a multifunctional receptor and chaperone coordinating cell–cell interactions and metabolic coupling. It regulates extracellular matrix remodeling by inducing matrix metalloproteinases, supports monocarboxylate transporter trafficking for lactate transport, and participates in signaling networks influencing proliferation, migration, and inflammatory responses. In mouse systems, Bsg activity intersects with pathways linked to hypoxia adaptation, angiogenic and stromal crosstalk, and immune cell recruitment. Dysregulated EMMPRIN/CD147 expression has been associated with tissue remodeling phenotypes and disease-relevant processes including tumor progression, fibrosis, and vascular dysfunction, making it a useful node for mechanistic studies.

EMMPRIN/CD147 Lentiviral Activation Particles (m) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Bsg upregulation across a broader range of human cell types.

EMMPRIN/CD147 Lentiviral Activation Particles (m) 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 Bsg transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous EMMPRIN/CD147 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Bsg 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.