Beta-Endorphin, rat

Beta-Endorphin, rat is a synthetic research peptide in the beta-endorphin / endogenous opioid peptide family. Beta-endorphin is a proopiomelanocortin-derived endogenous opioid peptide. Its N-terminal opioid sequence is required for strong receptor-binding and analgesic activity, while C-terminal residues modulate potency and peptide behavior. N-terminal acetylation, truncation, and residue substitution have therefore been used extensively to investigate opioid receptor recognition and beta-endorphin structure-activity relationships.

• mu- and delta-opioid receptor binding assays
• opioid peptide structure-activity studies
• proteolytic processing and stability experiments
• antibody and immunoassay controls
• analytical peptide standards

For fragments, substituted analogs, labeled peptides, stereochemical variants, or terminally modified forms, experimental behavior should be evaluated for the exact construct rather than assumed to match the native parent peptide. Sequence-dependent solubility, aggregation, adsorption, oxidation, and stability should be considered when establishing reconstitution, storage, and assay conditions.

1. Influence of N-terminal acetylation and C-terminal proteolysis on beta-endorphin activity
2. Primary structure and morphine-like activity of human beta-endorphin