This product is the C-terminal hexapeptide of BAM-12P, supplied as residues 7 to 12 of that sequence. The distinction that matters is what it lacks: the Tyr-Gly-Gly-Phe-Met opening of the parent peptide is absent, and with it the structural requirement for opioid receptor binding. The N-terminal tyrosine of an enkephalin is essential for opioid receptor recognition, so a fragment beginning after it is not expected to act as an opioid agonist. That makes this peptide a control reagent by construction rather than by substitution. Within the BAM series, the C-terminal region is where non-opioid activity resides, and the best-characterised example is BAM8-22, the corresponding fragment of the 22-residue member, which acts at sensory-neuron-specific Mas-related G protein-coupled receptors rather than opioid receptors. Fragments of this kind are how that separation was established experimentally. The practical use is therefore comparative. Running this hexapeptide alongside full-length BAM-12P (LT1041) at matched concentration attributes an observed effect either to the enkephalin N-terminus or to the C-terminal segment, which an opioid antagonist alone cannot fully resolve. Being short and lacking the enkephalin motif, it should not be assumed to reproduce the receptor pharmacology of the longer C-terminal fragments such as BAM8-22; establish its behaviour in the assay in use. | 