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NLP-2 (TRZ)
Synthetic 39-amino acid dual agonist peptide with binding affinity for GIP and GLP-1 receptor subtypes, incorporating a C20 fatty diacid moiety for extended albumin binding. Lyophilized, mass-spec certified, research-grade.
Frequently researched together
Technical specifications
NLP-2 (TRZ) is a synthetic 39-amino acid peptide engineered as a dual agonist of the glucose-dependent insulinotropic polypeptide (GIP) receptor and the glucagon-like peptide-1 (GLP-1) receptor — two incretin hormone receptors of the class B G-protein-coupled receptor family. GIP and GLP-1 are incretin hormones secreted from intestinal K-cells and L-cells respectively in response to nutrient ingestion, and their receptors are expressed across pancreatic islets, the central nervous system, and adipose tissue. The peptide carries a C20 fatty diacid moiety conjugated near the Lys20 residue, which enables reversible binding to serum albumin and extends the circulating half-life in pharmacokinetic model studies. Receptor pharmacology studies describe the molecule as an "imbalanced" and biased agonist — engaging the GIP receptor to a greater degree than the GLP-1 receptor, and preferentially driving cAMP signaling over β-arrestin recruitment at the GLP-1 receptor. As a research compound it is used to study dual-incretin receptor binding kinetics, comparative signal transduction, and incretin-axis pharmacology in vitro and in preclinical models.
- Single 39-amino acid peptide that activates both the GIP and GLP-1 receptors — two distinct incretin hormone receptors — from one molecule
- GIP (glucose-dependent insulinotropic polypeptide) and GLP-1 (glucagon-like peptide-1) are incretin hormones secreted by intestinal K-cells and L-cells; both receptors are class B G-protein-coupled receptors
- A C20 fatty diacid moiety conjugated near Lys20 promotes reversible serum-albumin binding, extending circulating half-life in pharmacokinetic model studies
- Characterized in receptor pharmacology studies as an "imbalanced" agonist — greater engagement of the GIP receptor than the GLP-1 receptor — with biased GLP-1 receptor signaling favoring cAMP generation over β-arrestin recruitment
- The peptide backbone is derived from the GIP sequence with substitutions that add GLP-1 receptor activity and increase resistance to dipeptidyl peptidase IV (DPP-IV) degradation
- Studied in published clinical research (the SURPASS and SURMOUNT trial programs) using pharmaceutical-grade formulations under clinical trial conditions, which are distinct from this RUO compound
- Lyophilized; reconstituted with bacteriostatic water for in vitro or animal model studies
- For research use only — not for human or veterinary administration
Peer-reviewed research
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