Not CRISPR data: the image illustrates antibody quality for visualizing CRISPR experiment results.
Not CRISPR data: the image illustrates antibody quality for visualizing CRISPR experiment results.
FBP1 Lentiviral Activation Particles (m): sc-424568-LAC
- Target species: mouse
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- FBP1 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
- FBP1 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 FBP1 Lentiviral Activation Plasmid (m) and FBP1 Lentiviral Activation Plasmid (m2) target distinct regulatory regions of the Fubp1 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: FBP1 Antibody (G-8): sc-271241
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
FBP1 Lentiviral Activation Particles (m) | sc-424568-LAC | 200 µl | $455.00 |
Mouse Fubp1 encodes far upstream element binding protein 1 (FBP1), a single-stranded DNA/RNA-binding regulator that couples transcriptional control with post-transcriptional RNA metabolism. FBP1 interacts with far-upstream promoter elements to modulate RNA polymerase II–dependent transcription and can influence mRNA stability and translation through binding to structured nucleic acids. Through these activities, Fubp1 contributes to programs governing cell-cycle progression, stress-responsive gene expression, and lineage-specific transcriptional states. Dysregulation of FUBP1-linked regulatory networks has been associated with altered growth control and differentiation phenotypes in disease-relevant contexts, supporting mechanistic studies in oncogenic and neurodevelopmental pathways.
FBP1 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 Fubp1 upregulation across a broader range of human cell types.
FBP1 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 Fubp1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous FBP1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Fubp1 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.