Integrin αM/CD11b Lentiviral Activation Particles (h): sc-400563-LAC

ITGAM encodes integrin αM (CD11b), which heterodimerizes with integrin β2 (CD18) to form Mac-1/CR3, a major adhesion and pattern-recognition receptor on myeloid cells. CD11b regulates leukocyte adhesion, transmigration, and phagocytosis by engaging ligands such as ICAMs, iC3b, and fibrinogen and coordinating outside-in signaling with cytoskeletal remodeling. Through integrin signaling and crosstalk with complement and innate immune pathways, ITGAM influences inflammatory activation states, reactive oxygen species production, and clearance of opsonized targets. Dysregulated ITGAM activity and expression are implicated in immune-mediated inflammation and infection biology, making it a frequent marker and mechanistic node in studies of myeloid cell function and tissue infiltration.

Integrin αM/CD11b 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 ITGAM upregulation across a broader range of human cell types.

Integrin αM/CD11b 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 ITGAM transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Integrin αM/CD11b expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ITGAM 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.