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CAT# Product Name M.W Molecular Formula Inquiry
L04002 Leucokinin II 850.9 C39H50N10O12 Inquiry
L04003 Leucokinin III 908.9 C40H52N12O13 Inquiry
L04005 Leucokinin V 782.8 C35H46N10O11 Inquiry
L04006 Leucokinin VII 864.9 C40H52N10O12 Inquiry
L04007 Leucokinin I 891.94 C42H52N10O11 Inquiry
L04008 LeucoPyr-okinin (LPK) 931.1 C42H66N12O12 Inquiry
L05001 LeucoPyr-okinin 931.06 C42H66N12O12 Inquiry
L05002 LeucoPyr-okinin (4-8) 631.78 C30H49N9O6 Inquiry


Leucokinins are a group of functionally diverse neuropeptides, 6 to 15 amino acids in length, that were first isolated from Leucophaea maderae based on their ability to stimulate hindgut contractions. Previous studies have shown that leucokinin is expressed in the brain and ventral ganglion of Drosophila central nervous system. The leucokinin neuropeptide plays a role in the neural network of the brain that modulates chemosensory response behavior. Neuropeptides of the leucokinin family, which are actually widely distributed throughout the insecta, are a type of hormone that induces fluid secretion from Malpighian tubules and has myotropic effects on the hindgut. These two features are shared with the peptide family of kinins.

Mechanism of action

In isolated Malpighian tubules of the yellow fever mosquito Aedes aegypti, leucokinins depolarize the transepithelial voltage. This effect on voltage is dependent on extracellular Cl. Although it is now clear that the dipteran leucokinins act on the Malpighian tubule stellate cells, the receptor(s) that mediates the leucokinin functions in mosquitoes and in insects, in general, is still unknown. The three Aedes leucokinins depolarize the transepithelial voltage in Malpighian tubules of A. aegypti at concentrations of less than 10-9 M; however only at concentrations above 10-8 M do they begin to show hindgut myotropic activity.

Application of Leucokinins

Leucokinins may be widely distributed in insects where they may have diverse functions in a variety of organs. Synthetic leucokinins have biological activity in a different insect and in a different tissue. One leucokinin, LK-8, the effects of which were studied further in isolated Malpighian tubules, was found to inhibit transepithelial fluid secretion at low concentrations and to stimulate fluid secretion at high concentrations.


  1. Blockade of the release of the neuropeptide leucokinin to determine its possible functions in fly behavior: Chemoreception assays. Begoña López-Arias., Belén Dorado., Pilar Herrero. (2011). Peptides, 32(3), 545-552.
  2. Characterization of a leucokinin binding protein in Aedes aegypti (Diptera: Culicidae) Malpighian tubule. Patricia VPietrantonio., Grant EGibson., Allison AStreya., DavidPetzel., Timothy KHayes. (2000). Insect Biochemistry and Molecular Biology, 30(12), 1147-1159.
  3. Leucokinins, a new family of ion transport stimulators and inhibitors in insect Malpighian tubules.T.K.Hayes., T.L.Pannabecker., D.J.Hinckley., G.M.Holman., R.J.Nachman., D.H.Petzel., K.W.Beyenbach. (1989). Life Sciences, 44(18), 1259-1266.
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