PKC lambda/iota Lentiviral Activation Particles (m): sc-422263-LAC
- Target species: mouse
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- PKC lambda/iota Lentiviral Activation Particles (m) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
- PKC lambda/iota Lentiviral Activation Particles (m) contain the following SAM Activation elements: a deactivated Cas9 (dCas9) nuclease (D10A and N863A) fused to the transactivation domain VP64, an MS2-p65-HSF1 fusion protein and a target-specific 20 nt guide RNA. They also contain the blasticidin, hygromycin and puromycin resistance genes
- Upon transduction, the SAM complex binds to a site-specific region approximately 200-250 nt upstream of the transcriptional start site and provides robust recruitment of transcription factors for highly efficient gene activation
- gRNAs encoded by PKC lambda/iota Lentiviral Activation Plasmid (m) and PKC lambda/iota Lentiviral Activation Plasmid (m2) target distinct regulatory regions of the Prkci promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: PKC lambda/iota Antibody (E-7): sc-376344
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
PKC lambda/iota Lentiviral Activation Particles (m) | sc-422263-LAC | 200 µl | $455.00 |
Mouse Prkci encodes atypical protein kinase C lambda/iota (PKCλ/ι), a serine/threonine kinase that functions as a core component of the PAR polarity complex to establish apical–basal polarity and coordinate asymmetric cell division. PKCλ/ι integrates cues from PI3K- and small GTPase–regulated signaling to control cytoskeletal organization, vesicle trafficking, and tight junction assembly, thereby shaping epithelial architecture and barrier function. Through phosphorylation-dependent control of transcriptional programs and cell-cycle regulators, Prkci influences proliferation, differentiation, and survival in context-dependent ways. Dysregulation of polarity and atypical PKC signaling has been linked to altered tissue homeostasis and oncogenic phenotypes, making Prkci a useful node for studying mechanisms of transformation, invasion, and developmental defects in mouse models.
PKC lambda/iota Lentiviral Activation Particles (m) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Prkci upregulation across a broader range of human cell types.
PKC lambda/iota Lentiviral Activation Particles (m) 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 Prkci transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PKC lambda/iota expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Prkci 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.