Eel calcitonin is a 32-residue fish calcitonin with a Cys1-Cys7 disulfide bond and C-terminal amidation. Its sequence shares substantial similarity with salmon and chicken calcitonins while retaining a distinct C-terminal region.

The peptide is useful for comparative calcitonin receptor studies and for investigating how naturally occurring sequence differences influence endocrine and cellular responses.

Product Information

A Distinct Fish Calcitonin Sequence

Eel calcitonin retains the highly conserved N-terminal ring found across the family but differs from salmon calcitonin in several residues toward the C-terminus.

This creates a useful natural comparison for structure–activity studies in which global peptide architecture is conserved while local sequence chemistry changes.

Pituitary and Receptor Signaling Research

Eel calcitonin has also been used experimentally outside classical bone models. Studies in cultured anterior pituitary cells have reported concentration-dependent effects on phosphoinositide signaling and prolactin release.

These observations make the molecule useful when calcitonin-family signaling is being examined across different endocrine cell systems rather than only through osteoclast endpoints.

Experimental Planning

We recommend comparing eel, salmon and mammalian calcitonins under matched receptor expression and assay conditions. Relative potency can change substantially with cell type, receptor isoform and endpoint timing.

Custom species variants can be evaluated through our Chemical Peptide Synthesis capabilities.

Frequently Asked Questions

Is eel calcitonin the same sequence as salmon calcitonin?

No. They share the same 32-residue architecture but differ at several positions, especially toward the C-terminal region.

Is eel calcitonin amidated?

Yes. The mature peptide terminates in Pro-NH₂.

Research Use Only.