CRABP-I Lentiviral Activation Particles (h2): sc-405485-LAC-2

Human CRABP1 encodes cellular retinoic acid-binding protein 1 (CRABP-I), a high-affinity cytosolic carrier that regulates intracellular retinoic acid availability and buffering, shaping retinoid gradient dynamics and downstream retinoic acid receptor signaling. By controlling retinoid partitioning and metabolism, CRABP-I influences transcriptional programs linked to cell differentiation, proliferation, and developmental patterning, and interfaces with processes such as neuronal function and inflammatory signaling. Altered CRABP1 expression and retinoid handling have been reported in contexts relevant to cancer biology, neurodevelopmental and neurodegenerative phenotypes, and metabolic dysregulation, making it a useful node for mechanistic studies. Gene editing of CRABP1 supports pathway dissection of retinoid transport and RA-responsive gene networks, enabling targeted perturbation experiments in cellular models to evaluate phenotypic consequences and regulatory circuitry.

CRABP-I 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 CRABP1 upregulation across a broader range of human cell types.

CRABP-I 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 CRABP1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous CRABP-I expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native CRABP1 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.