LIMP II Lentiviral Activation Particles (h): sc-402532-LAC

SCARB2 encodes lysosomal integral membrane protein 2 (LIMP II), a multi-pass membrane glycoprotein enriched on late endosomes and lysosomes that supports endolysosomal trafficking and lysosome homeostasis. LIMP II acts as a key receptor for delivery of β-glucocerebrosidase (GCase) to lysosomes, linking SCARB2 function to sphingolipid metabolism and proteostasis within the autophagy–lysosome pathway. Through its roles in membrane organization and cargo transport, SCARB2 influences processes such as endocytosis, lysosomal enzyme sorting, and degradation of macromolecules. Altered SCARB2/LIMP II activity has been associated with lysosomal storage phenotypes and neurodegeneration-related cellular stress, making it a relevant target for mechanistic studies of lysosome dysfunction and lipid catabolism.

LIMP II 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 SCARB2 upregulation across a broader range of human cell types.

LIMP II 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 SCARB2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous LIMP II expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native SCARB2 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.