Calcitonin (8-32) (salmon I)

Calcitonin is a hormone known to participate in calcium and Prus metabolism. Calcitonin (8-32) (salmon I) has been been proposed as an amylin receptor antagonist which is highly selective for amylin. It reverses the inhibitory effect of amylin on glucose-induced insulin release and potentiates the insulin response to glucose in the rat perfused pancreas.

Calcitonin (8-32) (salmon I) is a synthetic research peptide in the calcitonin family. The listed sequence/design is Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Thr-Gly-Ser-Gly-Thr-Pro-NH2. Calcitonin peptides are ligands for the calcitonin receptor. Structure-activity studies on salmon and human calcitonins have demonstrated important roles for the N terminus, central helical region, and C-terminal residues.

• receptor or binding assays
• competition experiments
• enzymatic-processing studies
• antibody or antigen controls
• analytical method development
• LC-MS/HPLC reference work
• comparative structure-activity experiments

Because this product may be a fragment, substituted analog, stereochemical variant, or terminally modified form, its activity should not be assumed to be identical to the native parent peptide. Peptide solubility, aggregation, adsorption to surfaces, and stability can vary with sequence, concentration, pH, ionic strength, and terminal modifications, so assay-specific reconstitution and storage conditions should be validated experimentally.

1. Structural determinants of salmon calcitonin bioactivity (PMID 16766525).
2. N-terminal truncation of salmon calcitonin leads to calcitonin antagonists (PMID 1325797).