PULSin® consists of a proprietary cationic amphiphilic molecule that forms non-covalent complexes with proteins and antibodies. Once formed, these complexes enter cells via anionic cell-adhesion receptors and are released into the cytoplasm, where they disassemble. The process is non-toxic and enables the delivery of functional proteins.
0.4 ml of PULSin® delivery reagent is sufficient for 25 delivery experiments in 6-well plates or 100 experiments in 24-well plates.
PULSin® can deliver R-phycoerythrin, a fluorescent protein (240 kD), into the cytoplasm of up to 98% of cells. The protein is evenly distributed in the cytoplasm and excluded from the nucleus due to its size.
Antibodies are successfully delivered into mammalian cells and can recognize their target protein within the cytoplasm. PULSin® enabled the delivery of FITC-labeled anti-alpha-tubulin into the cytoplasm of 85% of HeLa cells. Similarly, anti-giantin labeled with Alexa Fluor® 488 was delivered to 98% of live HeLa cells, labeling the Golgi apparatus.
A comparison of PULSin® with two other protein delivery reagents shows higher protein delivery efficiency. Moreover, the amount of protein delivered per cell is greater with PULSin®, as demonstrated with R-phycoerythrin and FITC-anti-alpha-tubulin.
PULSin® saves time and effort compared to techniques like viral transduction or chemical conjugation. The reagent is ready-to-use and comes with a dilution buffer and a fluorescent control protein (R-phycoerythrin).
The protocol is fast – simply mix the reagent with the protein, incubate, and apply to cells. Cells can be analyzed as early as 4 hours after delivery.