FAT10 Lentiviral Activation Particles (h): sc-402682-LAC

Human UBD encodes FAT10 (also known as ubiquitin D), a ubiquitin-like modifier that is strongly induced by pro-inflammatory cues such as TNF-α and IFN-γ. FAT10 covalently conjugates to substrate proteins and promotes their recognition by the 26S proteasome in a largely ubiquitin-independent manner, linking immune signaling to regulated protein turnover. Through effects on proteostasis, cell-cycle control, and stress responses, FAT10 influences pathways including proteasomal degradation and inflammatory transcriptional programs. Dysregulated UBD/FAT10 expression has been associated with chronic inflammation and oncogenic phenotypes, supporting its use as a molecular entry point for studying inflammation-cancer interfaces and immune-driven remodeling of the proteome.

FAT10 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 UBD upregulation across a broader range of human cell types.

FAT10 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 UBD transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous FAT10 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native UBD 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.