GLP-2 TZ  ·  Dual-Incretin Research Reagent

The dual-incretin
analog examined
across metabolic research.

A dual-receptor peptide that engages both the GIP and GLP-1 pathways simultaneously - the two key incretin signals studied in glucose handling, appetite regulation, and lipid metabolism. The most extensively characterised dual-incretin compound in this catalog.

Dual GIP / GLP-1 agonist39 residues≥99% HPLCC20 diacid acylation

Compound characterisation data. For Research Use Only - Not for Human Consumption.

GIPR ~1 nM GLP-1R ~3-5 nM GLP-2 TZ 39 amino acids GIP backbone Full agonism = native GIP cAMP-biased signaling C20 diacid ~120 hr half-life
99%
HPLC purity, every lot
Third-party verified · COA on file
2
Receptors engaged - GIPR + GLP-1R
Dual-incretin backbone
39
Residues in the peptide backbone
C20 diacid at Lys20
120 hr
Modeled plasma half-life
Albumin-bound depot

>99% Purity Guaranteed

Verified every batch

Tested at Freedom Diagnostic

Independent 6-panel COA

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US-Formulated & Filled

Lyophilized & sealed domestically

Mechanism of Action

Two receptors.
One sequence.

GLP-2 TZ is a GIP analogue with GLP-1 activity engineered in - not the reverse. Its GIPR dominance is intentional, enabling engagement of both incretin receptors within a single 39-residue backbone. Characterised for its dual-agonist pharmacology.

GIPR - Primary
GIP Receptor
~1 nM
Equal affinity to native GIP
Direct adipocyte lipid metabolism
Insulin sensitization & adiponectin
Lower GI side-effect profile observed vs GLP-1 monoagonists in published trials
GLP-1R - Biased
GLP-1 Receptor
~3–5 nM
~5x weaker, cAMP-biased
Preferential cAMP, less desensitization
Hypothalamic appetite suppression
Glucose-dependent insulin release
Why weaker GLP-1R affinity still wins
Cryo-EM (PNAS 2022) confirms biased cAMP signaling at GLP-1R reduces receptor internalization - sustained surface expression = prolonged effect. GIPR tolerability allows full dose escalation, delivering more total GLP-1R activation than selective agonists at their tolerable ceiling.
GIP backbone - not GLP-1
C20 diacid at Lys20 - ~120 hr t½
Aib2 - DPP-IV resistant
39 amino acids - 4,813 Da
Cryo-EM confirmed biased GLP-1R
Integrated signaling cascade
1
GIPR Full Agonism GIP
Equal affinity to native GIP. C20 diacid at Lys20 drives albumin binding, extending half-life to ~120 hr without sacrificing GIPR potency.
2
Biased GLP-1R Activation GLP-1
~5x weaker but cAMP-preferential. Tyr1 and C20 lipid destabilize beta-arrestin coupling - less internalization, sustained receptor surface expression.
3
Synergistic cAMP Elevation Both
Both receptors converge on adenylate cyclase. Dual Gs input produces synergistic beta-cell insulin secretion beyond GIP + GLP-1 administered separately.
4
Systemic Downstream Signaling Both
Adipocyte remodeling (GIPR), hypothalamic GLP-1R engagement, altered lipid metabolism, and inflammatory marker changes.

JCI Insight 2020 · PNAS 2022 · Nature Comms 2022

Molecular Architecture

39 residues.
Drawn to scale.

GLP-2 TZ's 39-amino-acid backbone, rendered residue-by-residue. Key engineering sites - Aib2 (DPP-IV block), Lys20 (C20 acylation), and the GLP-1-like C-terminal - highlighted as they appear.

GIP-native residues
Engineered GLP-1 residues
Shared / structural
Key modification site

Illustrative schematic · Research use only.

Receptor Selectivity Profile

Binding affinity
visualized.

GLP-2 TZ's dual-receptor engagement profile vs GLP-1 S (GLP-1 monoagonist). EC50 values from in vitro cAMP assays. Lower EC50 = higher affinity.

Axes = receptor binding affinity (higher = stronger). Research use only.

Pharmacokinetic Profile

Half-life by
molecular design.

The C20 fatty diacid at Lys20 drives albumin binding, extending modeled plasma half-life from <2 minutes (native GIP/GLP-1) to ~120 hours. Curve draws on scroll.

GLP-2 TZ ~120 hr
GLP-1 S ~168 hr
Native GIP/GLP-1 ~2 min

Modeled one-compartment PK. Research use only.

Compound Profile

Full specification

39-amino acid GIP analogue engineered for dual receptor co-activation. Built from the GIP sequence up - not adapted from GLP-1.

Structural Features
Key engineering modifications on the native GIP backbone
GIP-native Shared Engineered GLP-1 C-terminal Aib2 DPP-IV block Lys20 C20 fatty diacid C20 acyl chain albumin binding → ~120 hr t½ GIP-native Shared Engineered GLP-1 C-terminal
Common NameGLP-2 TZ
CodeLY3298176
Backbone39-aa GIP analogue - not GLP-1
Mol. Weight4,813.5 Da
EC50 GIPR~1 nM - equal to native GIP
EC50 GLP-1R~3–5 nM - cAMP-biased
Half-life~120 hr via C20 diacid albumin binding
DPP-IVResistant - Aib2 substitution at position 2
Reference ApprovalsT2D 2022Obesity 2023OSA 2024
Eon Purity≥99% HPLC - 6-panel COA every batch
FormLyophilized powder · sealed vial
RegulatoryResearch Use Only - Not for Human Use
Receptor Binding Affinity
GIPR-dominant by design. The imbalance is intentional and pharmacologically critical.
GIPR
~1 nM
GLP-1R
~3–5 nM
Biased cAMP signaling at GLP-1R compensates for weaker affinity. Research use only.
GIP Backbone - Built from Native GIP
GIP-unique residues give full GIPR agonism; engineered GLP-1-like residues add GLP-1R activity. One molecule, two native-affinity pathways.
C20 Fatty Diacid at Lys20
Longer chain than GLP-1 S (C18 at Lys26). Mid-sequence attachment preserves GIP-native N-terminal GIPR binding geometry. ~120 hr half-life.
Biased GLP-1R Signaling
Cryo-EM (PNAS 2022): Tyr1 and C20 moiety destabilize beta-arrestin coupling. Less internalization = sustained receptor surface expression = prolonged signaling.