$452.00 - $452.00
Exendin-4 (Glu1) is an N-terminally modified Exendin-4 analog designed for studies of how residue 1 contributes to glucagon-like peptide-1 receptor recognition and activation.
The N-terminal region of Exendin-family peptides enters the transmembrane receptor-binding cavity and plays a central role in coupling peptide recognition to G-protein activation. Altering this region therefore provides a direct way to examine receptor activation separately from the broader binding contributions of the peptide scaffold.
Product Information
| Property | Specification |
|---|---|
| Product Name | Exendin-4 (Glu1) |
| Peptide Class | Exendin-4 N-terminal analog |
| Modification | Glu at position 1 |
| Parent Scaffold | Exendin-4 |
| Research Target | GLP-1 receptor |
| Research Areas | Receptor activation, peptide SAR, class B1 GPCR pharmacology |
Why Residue 1 Matters
Structural and pharmacological studies of GLP-1R show that the peptide N-terminus interacts with the receptor transmembrane domain and contributes directly to activation of the receptor–G-protein complex.
A defined residue-1 substitution can therefore reveal changes in signaling efficacy that may not parallel changes in overall receptor affinity.
Sequence–Function Studies
Exendin-4 (Glu1) can be compared with full-length Exendin-4 and N-terminal truncation variants to examine how local chemistry influences cAMP signaling, receptor engagement and downstream pathway activation.
We recommend using matched receptor-expression conditions and including native Exendin-4 as the primary reference ligand in quantitative SAR experiments.
Analytical Considerations
Because the experimental value of this analog depends on its exact substitution pattern, sequence identity should be confirmed by mass spectrometry before quantitative receptor studies.
Our Peptide Quality Control capabilities support HPLC and mass-spectrometric characterization according to the selected specification.