
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
HYAL4 CRISPR Activation Plasmid (h) | sc-409245-ACT | 20 µg | $397.00 |
Human HYAL4 encodes a hyaluronidase-family enzyme implicated in extracellular matrix glycosaminoglycan turnover, influencing the remodeling of hyaluronan-rich microenvironments. By modulating pericellular matrix composition, HYAL4 can affect cell–matrix interactions, migration, and signaling outputs linked to adhesion and inflammatory responses. Altered hyaluronan metabolism has been associated with tissue fibrosis, tumor–stroma dynamics, and immune cell trafficking, making HYAL4 expression a relevant variable in disease-context models. Studying HYAL4 regulation and function helps clarify how glycan catabolism integrates with extracellular matrix homeostasis and cell behavior.
HYAL4 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous HYAL4 expression without altering the underlying DNA sequence.
HYAL4 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the HYAL4 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 HYAL4 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous HYAL4 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native HYAL4 locus and enabling the study of HYAL4-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of HYAL4 pathway restoration in tumor cells with silenced or reduced HYAL4 expression.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.