BMP-4 Lentiviral Activation Particles (h): sc-400543-LAC

Human BMP4 encodes bone morphogenetic protein 4 (BMP-4), a secreted TGF-β superfamily ligand that signals through type I/II BMP receptors to activate SMAD1/5/8 and downstream transcriptional programs. BMP-4 regulates embryonic patterning, mesoderm induction, osteogenic and chondrogenic differentiation, and lineage specification across multiple tissue contexts. Beyond canonical SMAD signaling, BMP-4 can intersect with MAPK, WNT, and NOTCH pathways to shape cell fate decisions, morphogenesis, and extracellular matrix remodeling. Dysregulated BMP4/BMP-4 activity has been implicated in developmental abnormalities and in disease-relevant processes such as fibrosis, vascular remodeling, and tumor microenvironment–associated differentiation cues, supporting its use in mechanistic pathway studies.

BMP-4 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 BMP4 upregulation across a broader range of human cell types.

BMP-4 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 BMP4 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous BMP-4 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native BMP4 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.