Sigma-Aldrich™ Melittin, >97% (HPLC), Calmodulin Binder, Lyophilized, 250 μg

Sigma-Aldrich™ Melittin is a 26-residue polypeptide isolated from bee venom and supplied as a high-purity (>97% HPLC) lyophilized powder. This amphipathic peptide exhibits membrane-disruptive, enzyme-modulating, and signaling activities that make it a valuable tool for cellular and molecular biology research.

Melittin binds calmodulin in a Ca²⁺-dependent manner, activates phospholipase A₂, and inhibits protein kinase C (IC₅₀ = 5–7 μM). It also modulates G-protein signaling, stimulating Giα and G11α activity while inhibiting Gs activity, and has been widely used for affinity purification of Ca²⁺-binding proteins.

Key Features

• High purity – >97% (HPLC).
• Defined sequence – H-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-NH₂.
• 26-residue peptide from bee venom.
• Biochemical activity – binds calmodulin (Ca²⁺-dependent), activates phospholipase A₂, inhibits PKC.
• Research-grade – RUO (Research Use Only).
• Lyophilized powder – stable and easy to handle; soluble in water (1 mg/mL).

Applications

• Study of signal transduction pathways involving calmodulin, PKC, and G-proteins.
• Enzyme activity modulation – activator of phospholipase A₂, inhibitor of protein kinase C.
• Affinity purification of Ca²⁺-binding proteins.
• Research in membrane biology – peptide-lipid interactions and permeabilization assays.
• Biochemical pharmacology studies of adenylate cyclase inhibition and Gi/Go modulation.

Technical Specifications

Sigma-Aldrich™ Melittin is a well-characterized, high-purity polypeptide with established activity on calmodulin, protein kinases, phospholipase A₂, and G-proteins. Its membrane-active properties and role in signaling make it an indispensable peptide for research in cell biology, neurobiology, biochemistry, and pharmacology.