Waglerin-1, recombinant venom peptide

Waglerin-1 venom peptide is a recombinant peptide purified from Escherichia coli that was originally isolated from the venom of Tropidolaemus wagleri (Temple pit viper). Waglerins are a group of four small peptides (waglerin-1, waglerin-2, waglerin-3 and waglerin-4) that were isolated from the venom of Temple pit viper. These small peptides are described as antagonists of the nicotinic acetylcholine receptor (nAChR) and have long been used as tools for the characterization of the nAChR. Waglerins block nAChR inhibiting the acetylcholine ligation to receptor. Several studies report that these small peptides cause paralysis and death by respiratory failure (Molles et al. , 2002). Waglerin-1 peptide was described as a selective inhibitor that blocks the epsilon form of the nAChR. Additional evidences indicate that waglerin-1 peptide also interact with GABAA receptors (Molles et al. , 2002). The recombinant peptide is provided in 50 mM NaHepes buffer, pH 7.5, 300 mM NaCl, at a 0.4 mg/mL concentration.Sequence: GGKPDLRPCY PPCHYIPRPK PR. Components: Waglerin-1, recombinant venom peptide. Shipping Conditions: Blue Ice. Storage Conditions: 2 °C to 8 °C. Application: Drug Discovery. Features: Number of Cysteines: 2, Number of Disulfide bonds: 1, Protein concentration: 0.4 mg/mL, Recombinant peptide purified from Escherichia coli. Product Category: Venom Peptides. Molecular Weight: 25,22 KDa