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Human α-CGRP (8-37) is a 30-residue C-terminal fragment of human α-CGRP used as a peptide antagonist in CGRP receptor pharmacology.
Removal of residues 1-7 eliminates the N-terminal disulfide ring associated with receptor activation while preserving much of the C-terminal binding interface.
Product Information
| Property | Specification |
|---|---|
| Product Name | Human α-CGRP (8-37) |
| CAS No. | 119911-68-1 |
| Sequence | Val-Thr-His-Arg-Leu-Ala-Gly-Leu-Leu-Ser-Arg-Ser-Gly-Gly-Val-Val-Lys-Asn-Asn-Phe-Val-Pro-Thr-Asn-Val-Gly-Ser-Lys-Ala-Phe-NH₂ |
| One-Letter Sequence | VTHRLAGLLSRSGGVVKNNFVPTNVGSKAF-NH₂ |
| Peptide Length | 30 amino-acid residues |
| Molecular Formula | C139H230N44O38 |
| Molecular Weight | Approximately 3125.6 Da |
| Disulfide Bond | None |
| Research Role | CGRP receptor antagonist |
Receptor Binding Without the Native Agonist Ring
The fragment preserves the human α-CGRP C-terminal sequence that contributes to receptor affinity but removes the cyclic N-terminal activation region.
This structural design explains why CGRP (8-37) became a useful ligand for receptor characterization and antagonist studies.
Human Versus Rat CGRP (8-37)
Human and rat fragments are not sequence-identical. The human peptide contains Asn25 and Lys35 in the corresponding full-length numbering, whereas the rat α-CGRP fragment contains Asp and Glu at those positions.
We recommend maintaining species consistency when antagonism is quantified in recombinant receptors or primary tissues.
Frequently Asked Questions
Is human CGRP (8-37) a 37-residue peptide?
No. It corresponds to residues 8 through 37 and therefore contains 30 amino acids.
Why does the peptide lack a disulfide bond?
The two cysteines in full-length CGRP are located within residues 1-7, which are absent from this fragment.