CRABP-II Lentiviral Activation Particles (h2): sc-402978-LAC-2

Human CRABP2 encodes cellular retinoic acid–binding protein II (CRABP-II), a high-affinity cytosolic carrier that buffers all-trans retinoic acid and facilitates its delivery to nuclear retinoic acid receptors to shape retinoid-dependent transcriptional programs. By controlling ligand availability and subcellular trafficking, CRABP-II influences epithelial differentiation, keratinocyte maturation, and other RA-driven processes, linking it to regulation of proliferation, apoptosis, and developmental gene networks. Dysregulated CRABP2 expression and altered retinoid signaling have been associated with cancer biology and inflammatory skin disorders, making this target relevant for studying pathway rewiring and context-specific RA responses. CRABP2-focused gene editing supports mechanistic dissection of retinoic acid signaling, mapping of transcriptional and chromatin changes downstream of RAR activation, and functional screening in differentiation and tumorigenesis models.

CRABP-II Lentiviral Activation Particles (h2) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient CRABP2 upregulation across a broader range of human cell types.

CRABP-II Lentiviral Activation Particles (h2) 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 CRABP2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous CRABP-II expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native CRABP2 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.