CCP2 Lentiviral Activation Particles (h): sc-410133-LAC

Human AGBL2 encodes CCP2, a cytosolic metallocarboxypeptidase that catalyzes deglutamylation of polyglutamylated proteins, including tubulin, thereby tuning microtubule dynamics and associated trafficking and mitotic processes. By reversing glutamylation marks written by tubulin tyrosine ligase–like enzymes, CCP2 helps regulate cilia-related functions, cytoskeletal remodeling, and the fidelity of motor protein interactions. Dysregulated tubulin post-translational modification homeostasis has been linked to altered cell migration, chromosomal instability, and signaling changes observed across multiple disease contexts, supporting the study of AGBL2/CCP2 in cancer biology and neurodevelopmental pathways. These features make AGBL2 a useful node for investigating microtubule-associated pathways, ciliary signaling, and post-translational modification networks.

CCP2 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 AGBL2 upregulation across a broader range of human cell types.

CCP2 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 AGBL2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous CCP2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native AGBL2 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.