
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
TMEM205 Lentiviral Activation Particles (h) | sc-408587-LAC | 200 µl | $455.00 |
TMEM205 encodes a multi-pass transmembrane protein that localizes to cellular membranes and has been implicated in regulating intracellular trafficking and membrane-associated transport processes. Altered TMEM205 expression has been linked to changes in cellular stress handling and drug transport phenotypes, making it relevant to studies of tumor cell adaptation and chemoresistance mechanisms. As a membrane protein with limited functional annotation, TMEM205 is frequently investigated using expression perturbation to define pathway connectivity, including effects on vesicle dynamics, membrane permeability, and cellular response programs. These features position TMEM205 as a useful target for functional genomics in cancer biology and cell physiology research.
TMEM205 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 TMEM205 upregulation across a broader range of human cell types.
TMEM205 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 TMEM205 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous TMEM205 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native TMEM205 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.