Melittin(Mellitin)

Synthetic melittin, the main component of the honeybee venom. The amphiphilic nature of this antimicrobial peptide makes it a excellent model compound for monitoring lipid-protein interactions in membranes. Integrates into cell membranes and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na(+)-K(+)-ATPase and the H(+)-K(+)-ATPase. Increases the permeability of cell membranes to ions, particularly Na+ and indirectly Ca(2+), because of the Na(+)-Ca(2+)-exchange. "

Melittin(Mellitin) is a 26-residue synthetic peptide with the sequence Gly-Ile-Gly-Ala-Val-Leu-Lys-Val-Leu-Thr-Thr-Gly-Leu-Pro-Ala-Leu-Ile-Ser-Trp-Ile-Lys-Arg-Lys-Arg-Gln-Gln. C-terminal amidation removes the terminal carboxylate charge. The sequence contains 3 Lys and 2 Arg residues, contributing cationic character; has a relatively high hydrophobic-residue fraction that can influence aqueous solubility and surface adsorption. These sequence-derived properties describe the reagent chemically; no specific receptor, enzyme, pathway, disease association, or biological activity is assigned without product-specific experimental evidence.

• LC-MS/HPLC analytical method development
• sequence-specific assay controls

Sequence-derived chemical properties support reagent selection and experimental planning but do not establish biological function. Solubility, aggregation, adsorption, conjugation efficiency, and assay performance should be validated under the intended experimental conditions.