
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
LARGE2 Lentiviral Activation Particles (h) | sc-414150-LAC | 200 µl | $455.00 |
Human LARGE2 encodes a Golgi-resident glycosyltransferase that contributes to post-translational glycosylation of extracellular and membrane proteins, including pathways governing matriglycan elaboration on α-dystroglycan. By modulating glycan structure, LARGE2 influences cell–matrix adhesion, receptor organization, and signaling events linked to basement membrane interactions and tissue integrity. Altered LARGE2 activity can perturb glycoprotein function and extracellular matrix communication, making it relevant to studies of dystroglycan glycosylation defects and broader glycosylation-associated phenotypes. LARGE2 expression is therefore frequently examined in models that connect Golgi glycosylation programs to neuromuscular and developmental biology.
LARGE2 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 LARGE2 upregulation across a broader range of human cell types.
LARGE2 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 LARGE2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous LARGE2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native LARGE2 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.