
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
HJURP CRISPR Activation Plasmid (h) | sc-405278-ACT | 20 µg | $397.00 |
HJURP (Holliday junction recognition protein) is a centromeric histone chaperone essential for accurate chromosome segregation. It mediates deposition and maintenance of the CENP-A histone H3 variant at centromeres, coordinating kinetochore assembly and mitotic progression as part of core centromere/kinetochore and DNA replication–coupled chromatin maintenance processes. Through its role in preserving centromere identity and genome stability, altered HJURP expression or function is frequently studied in the context of replication stress, aneuploidy, and proliferation-associated transcriptional programs. These features make HJURP a useful target for investigating mitotic fidelity, chromatin dynamics, and cancer-relevant cell cycle phenotypes in human cell models.
HJURP CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous HJURP expression without altering the underlying DNA sequence.
HJURP CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the HJURP 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 HJURP transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous HJURP expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native HJURP locus and enabling the study of HJURP-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of HJURP pathway restoration in tumor cells with silenced or reduced HJURP expression.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.