Tesamorelin 10mg

• 1. Overview
• 2. Biochemical Characteristics
• 3. Research Applications
• 4. Pathway / Mechanistic Context
• 5. Preclinical Research Summary
• 6. Form & Analytical Testing
• 7. Referenced Citations
• 8. RUO Disclaimer

Overview

Tesamorelin is a synthetic 44-amino acid analog of growth hormone-releasing hormone (GHRH), first described in published literature. Its defining structural feature is a trans-3-hexenoic acid modification conjugated to the N-terminus — a deliberate chemical addition designed to reduce proteolytic degradation at the N-terminal residue compared to native GHRH. The structural modification and its consequences for receptor binding kinetics are the central focus of the published pharmacology literature on this compound.

Tesamorelin binds at GHRH receptors (GHRHR) and activates downstream signaling pathways in the growth hormone axis. Published in vitro research has characterized the compound's receptor interaction profile and compared it to unmodified GHRH sequences to isolate the contribution of the N-terminal modification to receptor binding behavior. As a well-characterized GHRH analog with a substantial published literature base, Tesamorelin serves as a research tool for groups studying GHRH receptor pharmacology and growth hormone axis signaling in cell-based systems.

Biochemical Characteristics

Tesamorelin shares the 44-residue sequence of human GHRH(1–44) with the addition of a trans-3-hexenoic acid group at the N-terminal tyrosine residue. The trans-3-hexenoic acid modification is a short-chain unsaturated fatty acid conjugate that alters the electronic and steric environment of the N-terminus. Published work has characterized how this modification affects the rate of dipeptidyl aminopeptidase IV (DPP-IV) cleavage at the N-terminus, which is the primary proteolytic route for native GHRH inactivation in plasma.

The full sequence including modification yields molecular formula C₂₂₁H₃₆₆N₇₂O₆₇S, molecular weight 5136.12 g/mol. CAS 106612-94-6, PubChem CID 16137828. The GHRH backbone retains the helical structural elements responsible for GHRHR binding, while the N-terminal modification provides the stability advantage that makes Tesamorelin more tractable for in vitro assay work relative to native GHRH.

Research Applications

• GHRH receptor (GHRHR) binding characterization: radioligand competition assays and surface plasmon resonance studies examining binding affinity and kinetics
• Structure-activity relationship (SAR) studies: comparing Tesamorelin binding parameters to native GHRH(1–44) and truncated GHRH analogs to characterize the contribution of the N-terminal modification
• DPP-IV stability assays: enzymatic degradation kinetics comparing Tesamorelin vs. unmodified GHRH sequences under standardized assay conditions
• GHRHR downstream signaling studies: cAMP accumulation assays, PKA activation, and CREB phosphorylation in GHRHR-expressing cell lines
• Growth hormone axis research: cell-based models studying the signaling cascade downstream of GHRHR activation
• N-terminal fatty acid modification studies: mechanistic research on how short-chain fatty acid conjugation affects receptor interaction profiles in peptide pharmacology

All applications are restricted to non-clinical laboratory research environments.

Pathway / Mechanistic Context

GHRH receptors are Gs-coupled GPCRs. Binding at GHRHR activates adenylyl cyclase, elevating intracellular cAMP and activating protein kinase A (PKA). PKA activation drives phosphorylation of CREB and other downstream targets in the growth hormone signaling cascade. This pathway is well-characterized in the GHRHR cell biology literature, and Tesamorelin has been used as a research tool to study receptor activation kinetics and downstream signaling in cell-based assay systems.

The trans-3-hexenoic acid modification at the N-terminus has been studied specifically for its effect on DPP-IV resistance. DPP-IV cleaves peptides with a penultimate proline or alanine at position 2 from the N-terminus — native GHRH has a tyrosine-alanine N-terminal sequence that is susceptible to this cleavage. The N-terminal fatty acid conjugate in Tesamorelin sterically disrupts DPP-IV access, extending compound integrity in the enzymatic environment of the assay. Ionescu and Frohman (2006) characterized the pharmacokinetic profile of this modification class relative to unmodified GHRH, providing the mechanistic framework for interpreting Tesamorelin's stability advantage in published research.

Preclinical Research Summary

The published research base on Tesamorelin includes both in vitro pharmacology work and clinical research literature. For in vitro research purposes, the most directly relevant published work focuses on receptor binding characterization and stability assays. Ionescu and Frohman (2006, Journal of Clinical Endocrinology & Metabolism) characterized the receptor interaction profile and documented the DPP-IV stability advantage of the N-terminal trans-3-hexenoic acid modification, providing a mechanistic basis for interpreting the compound's behavior in cell-based assay systems.

Barake et al. (2018, Frontiers in Endocrinology) reviewed the broader GHRH analog pharmacology literature, placing Tesamorelin within the context of synthetic GHRH analog research and summarizing what is known about GHRHR binding characteristics across the analog series. This publication provides useful context for researchers designing GHRHR binding or signaling studies using Tesamorelin as a reference compound.

Form & Analytical Testing

Tesamorelin 10mg is supplied as research-grade lyophilized powder. Each batch is submitted to Vanguard Laboratory for conformity testing using a 5-vial protocol. The 7-panel protocol covers identity verification (mass spectrometry), purity analysis (≥98% via HPLC), net content verification (10mg confirmed), endotoxin levels, heavy metals screening, sterility, and overall conformity assessment. Batch-specific COAs are published on our COA Library and linked via QR code on each vial.

Referenced Citations

1. Ionescu M & Frohman LA, “Pulsatile secretion of growth hormone (GH) persists during continuous stimulation by CJC-1295, a long-acting GH-releasing hormone analog,” J Clin Endocrinol Metab, 2006 91(3):799–804.
2. Falutz J et al., “Effects of tesamorelin (TH9507), a growth hormone-releasing factor analog, in HIV-infected patients with excess abdominal fat,” N Engl J Med, 2010 363(23):2234–2244.
3. Barake M et al., “Growth hormone therapy and fracture risk,” Front Endocrinol, 2018 9:114.

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RUO Disclaimer

The products offered on this website are furnished for in-vitro studies only. In-vitro studies (Latin: in glass) are performed outside of the body. These products are not medicines or drugs and have not been approved by the FDA to prevent, treat or cure any medical condition, ailment or disease. Bodily introduction of any kind into humans or animals is strictly forbidden by law. This product should only be handled by licensed, qualified professionals.

This product is not a drug, food, or cosmetic and may not be misbranded, misused, or mislabeled as a drug, food, or cosmetic. No statements on this website have been evaluated by the FDA. You must be 21 years or older to purchase.

Batch COA: In Progress

This batch is currently undergoing conformity testing at Vanguard Laboratory. The full Certificate of Analysis — covering identity, purity (≥98% via HPLC), net content (10mg confirmed), endotoxins, heavy metals, and sterility — will be published here and linked via QR code on each vial upon completion.

We don't ship product before results are in. When the COA is live, you'll find it here and on our COA Library.