RTA-3 RT Peptide Analog

Research use only. Laboratory and investigational purposes — not for human or animal consumption.

Available to order · COA published for LOT#: RT-30-001 · View certificate

$179.00

FOR RESEARCH USE ONLY. Not for human consumption, medical use, or therapeutic application of any kind.

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SKU: DP-RTA3-001 Category:

FOR RESEARCH USE ONLY — Molecular Research Profile

RTA-3 RT — Molecular Research Profile

RTA-3 RT is a synthetic proglucagon-family peptide analog engineered to probe binding selectivity across GLP-1R (UniProt P43220), GIPR (UniProt P48546), and the glucagon receptor (GCGR; UniProt P47871) in multi-receptor panel assays, featuring backbone modifications at specified positions intended to differentiate receptor-contact contributions relative to native GLP-1, GIP, and glucagon pharmacophore sequences.

Molecular Architecture

Backbone
Proglucagon-family analog with sequence modifications at multiple positions to modulate tri-receptor selectivity; molecular weight in the 4,700–4,900 Da range by HPLC-MS characterization
Molecular weight
Confirmed single peak by ESI-MS at expected m/z; ≥99% HPLC purity (single molecular entity)
Secondary structure
Predicted N-terminal amphipathic α-helix (residues 1–~15) consistent with Class B GPCR engagement model; no disulfide bonds; fatty-acid acylation for serum-matrix stability
N-terminal
Native pharmacophore elements retained with position-specific substitutions to tune GLP-1R / GIPR / GCGR contact surfaces
Key note
A formally designated "GLP-3 receptor" is not assigned in the IUPHAR database; this compound is designed for receptor panel selectivity assays against GLP-1R, GIPR, and GCGR in parallel — not GLP-2R (UniProt P49190)

Receptor Binding and Signaling Mechanics

RTA-3 RT is characterized using multi-receptor panel assay formats across GLP-1R, GIPR, and GCGR (Class B1 GPCRs). Competitive radioligand displacement assays or homogeneous TR-FRET binding at membranes from cells overexpressing individual receptor subtypes allow selectivity profiling. All three receptors couple to Gαs, activating adenylyl cyclase and elevating intracellular cAMP, detectable by HTRF or AlphaScreen. Published triple-agonist pharmacophore work reports GIPR engagement at the lowest EC50 class, GLP-1R at intermediate concentrations, and GCGR requiring higher concentrations for full Emax — a pattern researchers replicate in individual-receptor cAMP assays.

Intracellular signaling cascade:

  1. Receptor panel binding: competitive displacement at GLP-1R / GIPR / GCGR membranes in parallel SPA or TR-FRET format
  2. Gαs → adenylyl cyclase → cAMP ↑ at each receptor individually (HTRF cAMP assay in receptor-overexpressing CHO-K1 or HEK293)
  3. cAMP → PKA → CREB Ser133 phosphorylation (Western blot or HTRF secondary endpoint)
  4. β-arrestin recruitment assay (BRET or PathHunter) in cells transfected with individual receptor constructs for biased-agonism characterization
  5. Reference agonists required in every panel: GLP-1(7-36)NH₂ (GLP-1R), GIP(1-42) (GIPR), glucagon (GCGR)

In Vitro Research Profile

Primary assay
Multi-receptor binding panel: radioligand displacement or homogeneous TR-FRET with fluorescent tracer at membranes from CHO-K1 cells stably expressing GLP-1R, GIPR, or GCGR individually
Functional assay
cAMP accumulation at each individual receptor; HTRF cAMP kit; 30-min incubation; full concentration-response from 1 pM to 10 µM
Cell lines
CHO-K1 or HEK293 stable transfectants expressing individual receptors; confirm expression by radioligand binding saturation before use
Concentration range
1 pM – 10 µM for selectivity profiling; include 8-point concentration series with 3-fold dilutions at each receptor
Known limitations
Published indexed-literature characterization specific to RTA-3 RT is limited; researchers should treat initial results as hypothesis-generating and include full reference agonist panels (GLP-1, GIP, glucagon) for data normalization

Research Use Only — Regulatory Notice

All compounds on this page are sold exclusively for in vitro laboratory research. They are not approved by the FDA, DEA, or any regulatory agency for human or animal use, therapeutic application, clinical investigation, or consumption of any kind. Binding affinities, IC50/EC50 values, and signaling cascade descriptions referenced herein derive from published in vitro and cell-based literature and do not constitute efficacy or safety claims. Researchers are responsible for complying with all applicable institutional, local, and federal regulations governing the handling and use of research chemicals.

Batch specifications

Compound
RTA-3 RT Peptide Analog
Net quantity
30 mg
Form
Lyophilized powder
HPLC purity
≥99%
Current lot
LOT#: RT-30-001
Testing panel
HPLC · Mass Spec · LAL Endotoxin
Storage
2–8°C, protected from light

Lot Documentation & Testing

Each lot is tested by HPLC (purity), mass spectrometry (identity confirmation), and LAL endotoxin assay prior to release. The Certificate of Analysis for this catalog lot is published below.

Description

FOR RESEARCH USE ONLY. Not for human consumption, medical use, or therapeutic application of any kind.

A synthetic peptide analog studied in vitro as a triple agonist of GLP-1R, GIPR, and the glucagon receptor (GCGR). In receptor-transfected cell cultures it has been characterized for activation of adenylyl cyclase and resulting cAMP accumulation across all three receptors, with published structural and pharmacology studies examining binding mode and relative potency in these in vitro systems.

Research Specifications

  • Purity: 99%+ (HPLC — Freedom Diagnostics)
  • Testing: HPLC · Mass Spectrometry · LAL Endotoxin
  • Form: Lyophilized powder
  • Storage: 2–8°C, protected from light

Why Researchers Choose This Catalog

  • Third-party verified purity — every batch, not sampled
  • Mass spectrometry confirmation of identity
  • Endotoxin-screened (LAL method)
  • QR code on each vial links to the published Freedom Diagnostics certificate for LOT#: RT-30-001 (view COA)
  • Lot-numbered inventory with corresponding batch documentation