PACAP 1-27 (BAT-006206)
* For research use only

Pituitary adenylate cyclase activating polypeptide (PACAP 1-27) is an endogenous neuropeptide showing considerable homology with vasoactive intestinal peptide (VIP). It is a potent PACAP receptor agonist.

Peptide Inhibitors
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PACAP 1-27
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Catalog Number Size Price Stock Quantity
BAT-006206 1 mg $398 In stock
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H-His-Ser-Asp-Gly-Ile-Phe-Thr-Asp-Ser-Tyr-Ser-Arg-Tyr-Arg-Lys-Gln-Met-Ala-Val-Lys-Lys-Tyr-Leu-Ala-Ala-Val-Leu-NH2; L-histidyl-L-seryl-L-alpha-aspartyl-glycyl-L-isoleucyl-L-phenylalanyl-L-threonyl-L-alpha-aspartyl-L-seryl-L-tyrosyl-L-seryl-L-arginyl-L-tyrosyl-L-arginyl-L-lysyl-L-glutaminyl-L-methionyl-L-alanyl-L-valyl-L-lysyl-L-lysyl-L-tyrosyl-L-leucyl-L-alanyl-L-alanyl-L-valyl-L-leucinamide
White lyophilised solid
Store in a cool and dry place (or refer to the Certificate of Analysis).
DMSO Solubility: 100 mg/mL (31.77 mM)
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1.A combination assay for simultaneous assessment of multiple signaling pathways.
Goetz AS;Liacos J;Yingling J;Ignar DM J Pharmacol Toxicol Methods. 1999 Dec;42(4):225-35.
We have developed an assay in which modulation of two or more signaling pathways can be assessed concurrently by combining reporter gene systems with fluorescent probe technology. The validation of this method was achieved by indirect analysis of adenylyl cyclase activation with the use of a cyclic AMP response element (CRE)-luciferase reporter system in combination with the measurement of calcium mobilization by Calcium Green-1 AM fluorescence on a fluorescent imaging plate reader. To demonstrate the utility of the method in studying the pharmacology of receptors that couple to more than one G protein, Chinese hamster ovary (CHO) cells, which stably expressed both the CRE-luciferase reporter gene and the human pituitary adenylyl cyclase-activating peptide (PACAP) receptor, were treated with PACAP 1-27 and 1-38. Calcium mobilization and the induction of adenylyl cyclase activity in response to each concentration of peptide were assessed in individuals wells. This assay may also be used to screen for ligands of two or more unrelated receptors simultaneously without compromising the assessment of either signaling pathway. To illustrate this point, Rat-1 fibroblasts, which expressed human alpha1A receptors, were cocultured with CRE-luciferase CHO cells, which expressed human GLP-1 receptors.
2.PACAP 1-38 as an inhaled bronchodilator in guinea pigs in vivo.
Lindén A;Cardell LO;Yoshihara S;Stjärne P;Nadel JA Peptides. 1998;19(1):93-8.
The effect on total pulmonary resistance (R1) was examined for inhaled PACAP 1-38, PACAP 1-27 and VIP in anesthetized, ventilated guinea pigs. Two minutes after inhalation, PACAP 1-38 (36 +/- 6%), PACAP 1-27 (42 +/- 9%) and VIP (48 +/- 19%) inhibited the increase in R1 (% inhibition of histamine-induced R1 prior to inhalation) caused by histamine i.v., whereas the vehicle (-1 +/- 10%) did not. This inhibitory effect lasted five times longer for PACAP 1-38 (> 50 min) than for PACAP 1-27 and VIP (< 10 min). The inhaled peptides caused no sustained effects on heart rate or blood pressure. Infusion of PACAP 1-38 i.v. dose-dependently inhibited the increase in R1 caused by inhaled histamine and by carbachol i.v..
3.Characterization and purification of the solubilized pituitary adenylate-cyclase-activating polypeptide-1 receptor from porcine brain using a biotinylated ligand.
Schäfer H;Schmidt WE Eur J Biochem. 1993 Nov 1;217(3):823-30.
A specific receptor for the brain-gut neuropeptide pituitary adenylate-cyclase-activating polypeptide (PACAP-1 receptor) was solubilized with Chapso from porcine brain plasma membranes and purified. Binding of 125I-PACAP(1-27) to the solubilized material was reversed equipotently by unlabeled PACAP(1-27) and PACAP(1-38). Soluble receptors retained the binding affinities and specificities of the plasma membrane fraction. Scatchard analysis of equilibrium-binding data indicated the existence of a single high-affinity binding site (Kd = 0.23 nM, Bmax = 1.2 pmol/mg protein). Binding of 125I-PACAP(1-27) to solubilized receptors was not affected by guanosine nucleotides, suggesting that solubilization dissociates the PACAP-1 receptor/guanosine-nucleotide-binding protein complex. Affinity cross-linking of 125I-PACAP(1-27) to soluble PACAP-1 receptors identified a specifically labeled 60-kDa protein. Enzymic deglycosylation of soluble affinity-labeled receptors reduced the apparent molecular mass by 10 kDa. The solubilized receptor glycoprotein was purified 4-5-fold by lectin-adsorption chromatography on wheatgerm agglutinin immobilized on agarose. S-Biotinyl[Ala28-34, Cys35]PACAP(1-35) was synthesized, immobilized on streptavidin-coated magnetic Sepharose beads and used to further affinity-purify wheatgerm-agglutinin-eluted receptor material.
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