Overview
- Lang, R. et al. (2005) Neuropeptides 39, 179.
Alomone Labs human GALP (3-32) activates Galanin 2 receptor-mediated Ca2+ mobilization in CHO-K1-Gα16-mt Aequorin cells.Dose response of normalized activation Galanin 2 receptor-mediated Ca2+ mobilization, evoked by human GALP (3-32) (#GPG-250). Ca2+ response was detected by measuring aequorin-derived fluorescence following application of human GALP (3-32) at different concentrations. The EC50 measured for human GALP (3-32) is 11.1 nM.
- Lang, R. et al. (2005) Neuropeptides 39, 179.
- Schmidhuber, S.M. et al. (2007) J. Invest. Dermatol. 127, 716.
Human GALP (3-32) fragment is a human galanin-like peptide that acts as a non-selective and potent galanin receptor agonist. Human GALP consists of 60 amino acid with a potential proteolytic cleavage site between two basic amino acids in position 33.
Human GALP (3-32) shares amino acids in position 9-21 with the first 13 amino acids of galanin, an essential sequence for activating galanin receptors1,2. Galanin receptors belong to the family of G-protein coupled receptors and consist of three subtypes: GalR1, GalR2, and GalR3.
Human GALP (3-32) is at least as potent as full length GALP. Studies suggest that GALP (3-32) fragment can represent the strongest mediator of biological GALP activity. GALP (3-32) can be used as a useful tool for studding the affinity of GALP to galanin receptors and to search for specific GALP receptors1,2. Human GALP (3-32) displays highest affinity to GalR3 with an IC50 value of 10 nM, followed by GalR2 with IC50 of 28 nM and GalR1 with IC50 of 77 nM1.
human GALP (3-32) (#GPG-250) is a highly pure, synthetic, and biologically active peptide.
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