Bid BH3-R8 combines the canonical Bid BH3 helical motif with an octa-arginine extension that enhances interaction with negatively charged membranes and biomolecules. The amphipathic helix supports high-affinity binding to hydrophobic protein grooves. Its cationic tail improves cellular association in model systems. Researchers use it to study helix-target recognition, membrane engagement, and peptide delivery mechanisms.
CAT No: T02001
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