CLEC-2D Lentiviral Activation Particles (h): sc-412035-LAC

CLEC2D encodes CLEC-2D, a C-type lectin-like ligand that engages the inhibitory receptor KLRB1/CD161 on NK cells and subsets of T cells, contributing to immune checkpoint-like regulation of cytotoxicity and cytokine production. By shaping NK–T cell crosstalk at the cell surface, CLEC-2D influences immune recognition within inflammatory and tumor-associated microenvironments and can affect responses to cellular stress. Altered CLEC2D expression has been associated with immune evasion phenotypes and dysregulated tissue inflammation, making it relevant to studies of immunosurveillance, tolerance, and leukocyte activation programs. CLEC-2D function is commonly investigated in contexts that link ligand–receptor signaling to transcriptional changes in effector cells and antigen-presenting or stromal compartments.

CLEC-2D 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 CLEC2D upregulation across a broader range of human cell types.

CLEC-2D 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 CLEC2D transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous CLEC-2D expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native CLEC2D 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.