GLP-1 SM

The molecule is a 31-residue peptide built on the GLP-1(7-37) scaffold with α-aminoisobutyric acid substitution at position 8 (conferring DPP-IV resistance) and a γ-glutamic-acid linker plus C18 fatty diacid acylation on the lysine at position 26. The fatty-acid moiety drives high-affinity reversible albumin binding, producing a pharmacokinetic profile documented in the literature as multi-day plasma residence — substantially longer than native GLP-1 or short-acting GLP-1R analogs. The molecule retains affinity for the GLP-1 receptor, a class B G-protein-coupled receptor that engages Gs-coupled cAMP signaling. Interaction profile in published work spans GLP-1R agonism, β-cell signaling investigations, and metabolic-pathway research in cell-culture and animal-model contexts. All activity descriptors here are framed as documented in published research. Structural confirmation is established by mass spectrometry and HPLC-validated purity on each Certificate of Analysis.

Experimental domains documented in the published literature include GLP-1 receptor binding-affinity studies, structure-activity work probing the role of fatty-acid acylation in albumin binding and receptor engagement, β-cell signaling investigations in pancreatic-islet preparations, metabolic-pathway research in animal-model contexts, comparative work alongside other GLP-1R agonist analogs (short-acting and long-acting), and screening assays for albumin-conjugated peptide pharmacokinetic characterization. Investigators have also characterized the molecule in studies of receptor desensitization kinetics and in cAMP-signaling assays in receptor-expressing cell lines. Use in laboratory research extends to mechanism-elucidation paradigms where the construct serves as a defined extended-residence GLP-1R agonist reference. The reference standard is supplied for these and equivalent in-vitro and animal-model experimental contexts only, with no associated guidance for human, clinical, or veterinary application.

Each lot is characterized by reverse-phase HPLC for chromatographic purity and by mass spectrometry for molecular-ion confirmation against the C187H291N45O59 empirical formula. Purity is reported as an HPLC-area percentage on the Certificate of Analysis distributed with every lot, alongside the molecular-weight match within instrument tolerance. The acylation site and fatty-diacid stoichiometry are confirmed by tandem mass spectrometry when included in the lot's release specification. Peptide content where applicable is determined by amino-acid analysis or nitrogen-content assay following the analytical method specified on the COA. Residual solvent and water content are reported categorically when these parameters are part of the lot's release specification. The COA records the lot identifier, manufacturing date, and analytical method versions used. Researchers requiring batch-level analytical detail should reference the COA distributed with the supplied material.

For laboratory storage, the lyophilized reference standard should be held at −20°C in its sealed, light-protected container until ready for analytical use. Allow vials to equilibrate to ambient temperature before opening to avoid moisture condensation on the lyophile. Reconstitution for in-vitro experimental use is typically performed in bacteriostatic water or a researcher-selected buffer compatible with the downstream assay; once reconstituted, store the working solution at 2–8°C and characterize stability in the relevant buffer prior to extended storage. Acylated peptide analogs may exhibit aggregation behavior in some buffer systems — assay-specific stability characterization is recommended. Avoid repeated freeze-thaw cycles of reconstituted material — single-use aliquots are preferred for experiments where peptide integrity is assay-critical. These handling parameters do not constitute preparation guidance for human or veterinary application.