LARP1 CRISPR Activation Plasmid (h): sc-404097-ACT

Human LARP1 (La ribonucleoprotein 1) is an RNA-binding protein that regulates mRNA stability and translation, with prominent effects on 5′TOP mRNAs encoding ribosomal proteins and translation factors. It functions at the interface of mRNP remodeling and ribosome biogenesis, integrating nutrient and growth cues through mTORC1-dependent signaling to modulate protein synthesis capacity. By shaping translational output and stress-adaptive gene expression programs, LARP1 contributes to control of cell growth, proliferation, and metabolic homeostasis. Dysregulated LARP1 activity and altered mTOR–translation networks have been reported in diverse disease contexts, supporting its use as a mechanistic node for studying translational control and cellular growth regulation.

LARP1 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous LARP1 expression without altering the underlying DNA sequence.

LARP1 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the LARP1 locus in human cell lines. The system is built around a catalytically inactive Cas9 (dCas9) carrying two inactivating mutations (D10A and N863A) that eliminate nuclease activity while preserving DNA binding. This dCas9 is fused to VP64, a potent transcriptional activator, and is co-expressed with a blasticidin resistance gene for selection. The second plasmid encodes the MS2-p65-HSF1 fusion protein, a secondary activator complex that works in concert with dCas9-VP64, alongside a hygromycin resistance gene. The third plasmid encodes a target-specific 20 nt sgRNA fused to two MS2 RNA aptamers that recruit the MS2-p65-HSF1 complex to the activation site, accompanied by a puromycin resistance gene. The three plasmids are delivered at a 1:1:1 mass ratio for balanced expression of all system components.

Once assembled at the target locus, the SAM complex binds within approximately 200 bp upstream of the LARP1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous LARP1 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native LARP1 locus and enabling the study of LARP1-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of LARP1 pathway restoration in tumor cells with silenced or reduced LARP1 expression.

For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.