$121.00 - $121.00
Biotin-Calcitonin, salmon I is an N-terminally biotinylated derivative of full-length salmon calcitonin. The construct retains all 32 residues, the Cys1-Cys7 disulfide ring and the C-terminal Pro-NH₂ while adding a streptavidin-compatible affinity handle.
This design enables calcitonin-family receptor studies to be combined with immobilization, capture or detection workflows.
Product Information
| Property | Specification |
|---|---|
| Product Name | Biotin-Calcitonin, Salmon I |
| Catalog No. | AS2625 |
| Sequence | Biotin-Cys-Ser-Asn-Leu-Ser-Thr-Cys-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 | Biotin-CSNLSTCVLGKLSQELHKLQTYPRTNTGSGTP-NH₂ |
| Peptide Length | 32 amino-acid residues |
| Molecular Formula | C155H254N46O50S3 |
| Molecular Weight | Approximately 3658.2 Da |
| Modification | N-terminal biotin |
| Disulfide Bond | Cys1-Cys7 |
Affinity Tag with the Native Ring Preserved
The biotin group is attached through the N-terminal amino functionality and does not require removal of the Cys1 thiol. The native Cys1-Cys7 disulfide architecture can therefore remain intact.
This is an important distinction from truncation-based probes such as salmon calcitonin (8-32).
Streptavidin-Based Assay Design
Biotin enables capture on streptavidin-coated surfaces or detection with streptavidin conjugates. Potential applications include ligand-binding experiments, immobilized peptide systems and receptor-interaction workflows.
We recommend experimentally comparing biotinylated and unlabeled salmon calcitonin when quantitative receptor kinetics are important because N-terminal derivatization can alter ligand behavior.
Frequently Asked Questions
Where is biotin attached?
The construct is N-terminally biotinylated at the beginning of the salmon calcitonin sequence.
Does the peptide retain the native disulfide ring?
Yes. The intended oxidized form contains the Cys1-Cys7 linkage.