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.
ABHD14B Lentiviral Activation Particles (h): sc-410211-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- ABHD14B Lentiviral Activation Particles (h) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
- ABHD14B Lentiviral Activation Particles (h) 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 ABHD14B Lentiviral Activation Plasmid (h) and ABHD14B Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the ABHD14B promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: ABHD14B Antibody (E-12): sc-515084
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
ABHD14B Lentiviral Activation Particles (h) | sc-410211-LAC | 200 µl | $455.00 |
ABHD14B (abhydrolase domain containing 14B) encodes a serine hydrolase–family protein implicated in regulating cellular lipid and small-molecule metabolism through ester/amide bond hydrolysis. As a member of the α/β-hydrolase fold superfamily, ABHD14B is positioned to influence metabolic homeostasis, organelle-associated lipid handling, and downstream signaling processes that can intersect with stress responses and inflammatory pathways. Expression and functional variation in ABHD family enzymes have been associated with altered bioenergetics and membrane lipid remodeling, features frequently observed in metabolic dysfunction and cancer-relevant cellular states. Accordingly, ABHD14B provides a tractable node for mechanistic studies linking hydrolase activity to pathway-level phenotypes in human cell models.
ABHD14B 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 ABHD14B upregulation across a broader range of human cell types.
ABHD14B 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 ABHD14B transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ABHD14B expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ABHD14B 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.