Alexa Fluor 488-Labeled GLP-1 (7-36) Peptide

Alexa Fluor 488-Labeled GLP-1 (7-36) Peptide contains the native human GLP-1(7-36) peptide sequence HAEGTFTSDVSSYLEGQAAKEFIAWLVKGR, followed by a glycine/serine-rich linker and a cysteine carrying Alexa Fluor 488.

GLP-1(7-36)

Glucagon-like peptide-1 (GLP-1) is an incretin peptide generated by tissue-specific processing of proglucagon. The mature GLP-1(7-36) sequence is widely used in receptor, enzymology, structure-function, and assay-development research.

GLP-1 acts through the GLP-1 receptor, a class B G-protein-coupled receptor. Native GLP-1 is also a substrate for dipeptidyl peptidase-4, making the unmodified native sequence useful for studies of receptor activation, peptide processing, ligand stability, and analytical method development.

Fluorescent GLP-1 Probe Design

The GGGSGGG spacer separates the GLP-1 sequence from the fluorescent cysteine label. This type of design can help reduce direct steric interference between the fluorophore and the native peptide sequence while providing a defined optical reporter.

Alexa Fluor 488 supports fluorescence-based studies such as receptor-binding assays, microscopy, flow cytometry, uptake studies, or assay development. Experimental behavior of a labeled derivative should be validated for each specific application because fluorophore and linker placement can influence receptor affinity or trafficking.

Potential Research Applications

• GLP-1 receptor binding
• GPCR trafficking and internalization
• Fluorescence microscopy
• Flow cytometry
• Ligand competition assays
• Peptide stability studies
• DPP-4 processing research

References

Amiram M, et al. A depot-forming glucagon-like peptide-1 fusion protein reduces blood glucose for five days with a single injection. J Control Release. 2013.
Public source / publication

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Research Use Only. Not for human, diagnostic, clinical, or therapeutic use.

Alexa Fluor 488-Labeled GLP-1 (7-36) Peptide is a synthetic research peptide in the glucagon-like peptide-1 (GLP-1) research peptide family. GLP-1 is an incretin peptide that activates the class B GLP-1 receptor. Structure-activity studies using substituted and truncated GLP-1 peptides demonstrated that defined residues contribute to receptor binding and cyclic-AMP signaling, while structural studies show a helical peptide conformation within the activated receptor complex. Modified GLP-1 variants are therefore useful for separating receptor binding from receptor activation and for comparing analog potency.

• GLP-1 receptor binding assays
• cAMP and receptor-signaling experiments
• incretin peptide structure-activity studies
• agonist/antagonist comparisons
• analytical peptide reference applications

For fragments, substituted analogs, labeled peptides, stereochemical variants, or terminally modified forms, experimental behavior should be evaluated for the exact construct rather than assumed to match the native parent peptide. Sequence-dependent solubility, aggregation, adsorption, oxidation, and stability should be considered when establishing reconstitution, storage, and assay conditions.

1. Structure-activity relationships of glucagon-like peptide-1(7-36)amide
2. Crystal structure of the GLP-1 receptor bound to a peptide agonist