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Salmon calcitonin (8-32) is a 25-residue C-terminal fragment of salmon calcitonin. The peptide begins at Val8 and therefore lacks the Cys1-Cys7 disulfide ring of full-length salmon calcitonin.
This truncation changes the molecule from a classical calcitonin agonist scaffold into a useful ligand for amylin and calcitonin-family receptor studies.
Product Information
| Property | Specification |
|---|---|
| Product Name | Calcitonin (8-32), Salmon I |
| Catalog No. | AS2643 |
| CAS No. | 155069-90-2 |
| Sequence | 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 |
| One-Letter Sequence | VLGKLSQELHKLQTYPRTNTGSGTP-NH₂ |
| Peptide Length | 25 amino-acid residues |
| Molecular Formula | C119H198N36O37 |
| Molecular Weight | Approximately 2725.1 Da |
| Disulfide Bond | None |
| C-Terminus | Pro-NH₂ |
Removing the Calcitonin Activation Ring
Full-length salmon calcitonin begins with a seven-residue disulfide-constrained region. Calcitonin (8-32) removes that entire segment while preserving the C-terminal receptor-recognition sequence.
The result is pharmacologically different from intact salmon calcitonin and should not be described as simply a shorter equivalent of the native agonist.
Amylin Receptor Research
Salmon calcitonin (8-32) has been used as an antagonist-oriented ligand in studies of amylin binding sites and amylin receptor pharmacology.
Its behavior can be compared with the more highly modified antagonist AC187 to investigate how N-terminal truncation and C-terminal substitutions affect receptor preference.
Frequently Asked Questions
Does salmon calcitonin (8-32) contain the Cys1-Cys7 ring?
No. Both cysteines are located in residues 1-7 and are absent from this fragment.
How many residues does this fragment contain?
It contains 25 residues, corresponding to positions 8 through 32.