
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
CCDC23 Lentiviral Activation Particles (h) | sc-415702-LAC | 200 µl | $455.00 |
SVBP encodes the small vasohibin-binding protein, also referred to as CCDC23, which functions as an essential cofactor for vasohibin proteins and supports their tubulin carboxypeptidase activity responsible for detyrosination of α-tubulin. Through regulation of microtubule post-translational modification, SVBP influences cytoskeletal dynamics, mitotic spindle organization, intracellular trafficking, and cell migration. Altered microtubule detyrosination has been implicated in defects in cell division and motility-associated phenotypes, providing a mechanistic link to pathways relevant to cancer biology and neurodevelopmental processes. As a result, modulation of SVBP/CCDC23 expression is useful for studying microtubule-dependent signaling, organelle transport, and cytoskeletal remodeling in human cells.
CCDC23 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 SVBP upregulation across a broader range of human cell types.
CCDC23 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 SVBP transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous CCDC23 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native SVBP 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.