
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
ZUFSP Lentiviral Activation Particles (h) | sc-415124-LAC | 200 µl | $455.00 |
ZUFSP (zinc finger with UFM1-specific peptidase domain) encodes a deubiquitinating enzyme that regulates protein homeostasis through protease activity toward ubiquitin-like modifiers. The ZUFSP protein has been linked to control of DNA damage response and replication-associated genome maintenance by modulating ubiquitin signals at stalled replication forks and repair intermediates. Through its role in coordinating ubiquitin-dependent processing, ZUFSP can influence chromatin-associated pathways, cell cycle progression, and cellular stress responses. Dysregulated ubiquitin signaling and impaired genome stability are recurrent features in cancer biology and neurodegeneration research, making ZUFSP a useful node for mechanistic studies of proteostasis and DNA repair.
ZUFSP 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 ZUFSP upregulation across a broader range of human cell types.
ZUFSP 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 ZUFSP transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ZUFSP expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ZUFSP 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.