Bid BH3-R9 fuses a BH3 helical domain with an arginine-rich extension that enhances cellular association and membrane interaction. The cationic tail promotes contact with negatively charged lipid surfaces and biomolecules. Its design supports evaluation of intracellular delivery and binding mechanisms. Research fields include peptide trafficking, helix-mediated recognition, and complex assembly studies.
CAT No: C08057
Synonyms/Alias:ARG-ARG-ARG-ARG-ARG-ARG-ARG-ARG-ARG-GLY-GLU-ASP-ILE-ILE-ARG-ASN-ILE-ALA-ARG-HIS-LEU-ALA-GLN-VAL-GLY-ASP-SER-MET-ASP-ARG;Bid BH3 - r9;RRRRRRRRRGEDIIRNIARHLAQVGDSMDR;RRRRRRRRRRGEDIIRNIARHLAQVGDSMDR
1. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
3. TMEM16F and dynamins control expansive plasma membrane reservoirs
5. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
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