This product supplies a longer segment of BID than the core BH3 construct (LT1051). The supplied sequence carries an additional N-terminal extension ahead of the BH3 helix, and the stated molecular weight is correspondingly higher, around 2310 against roughly 1839 for the shorter version. Length matters for this family for a structural reason. The BH3 motif is active as an amphipathic helix, and residues flanking the minimal motif contribute to how readily that helix forms and how stably it sits in the binding groove. Extended constructs frequently show greater helical propensity in solution than minimal ones, which is the same principle exploited by stapled BH3 peptides and by multivalent designs; work on Bid-BH3 peptide-oligosaccharide conjugates reported higher intracellular activity at matched overall peptide concentration, illustrating how presentation rather than sequence alone drives potency here. Functionally this remains a BID-derived activator peptide, engaging the effectors BAK and BAX rather than acting only as a sensitiser. The practical reason to choose this construct over the minimal one is when a more helical, higher-affinity reagent is wanted, for example in binding measurements or where the minimal peptide gives a weak signal. For a direct comparison of construct length under identical conditions, run it against LT1051. | 