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Peptide Library · Growth Hormone
Stabilized GHRH analog (modified GRF 1-44)

Tesamorelin

Also known as TH9507, Tesamorelin acetate

Tesamorelin is a stabilized analog of full-length GHRH(1-44) with an N-terminal hexenoyl modification. A research profile centered on the 44-residue backbone and what the acyl group does.

Tesamorelin sits at the more elaborate end of the GHRH-analog family. While sermorelin and CJC-1295 are built on the 29-residue GRF(1-29) core, tesamorelin is based on the full 44-amino-acid length of human GHRH, and it carries a distinctive chemical cap on its N-terminus.

It is also the most clinically characterized molecule in this group, which makes precision about what it is especially important on a research-use page. Here the focus is strictly structural and contextual — no therapeutic or dosing claims.

Composition

Tesamorelin is an analog of full-length human GHRH(1-44) carrying a trans-3-hexenoyl group attached to the N-terminal tyrosine. That N-terminal acylation is the structural feature that stabilizes the molecule against enzymatic degradation and distinguishes it from the shorter GRF(1-29)-based analogs.

A full-length GHRH backbone, capped

Human GHRH is naturally 44 amino acids long. Tesamorelin retains that full length rather than truncating to the 29-residue active fragment used by sermorelin and CJC-1295. Attached to its N-terminal tyrosine is a trans-3-hexenoyl group — a small unsaturated acyl cap.

That cap is the point of the molecule. The N-terminus of GHRH is a prime site for enzymatic attack; acylating it slows degradation and gives tesamorelin greater stability than the unmodified releasing hormone. It is a different stabilization strategy from CJC-1295's approach of internal amino-acid substitutions, and different again from the DAC form's albumin binding.

Same receptor, different structural class within it

For all its structural differences, tesamorelin acts through the same GHRH receptor as the rest of this family — the releasing-hormone side of the growth-hormone axis, distinct from the ghrelin receptor used by ipamorelin, the GHRPs, hexarelin and MK-677.

Its 44-residue length plus the acyl modification means it will not resolve to a short standard-residue list, and its mass on a certificate of analysis sits well above the GRF(1-29)-based analogs — a useful way to tell it apart from sermorelin and CJC-1295 on paper.

Studied in the context of
GHRH-receptor signalingFull-length GHRH(1-44) analog structureN-terminal acylation / peptide-stability modelsGH-axis research

These are research areas the compound is associated with in the literature — not medical claims or intended uses.

Handling & storage

Supplied lyophilized. Stored sealed and cold; reconstituted with bacteriostatic water only as a protocol requires, then refrigerated. Handle per accepted laboratory practice.

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Common questions

How is tesamorelin different from sermorelin?

Sermorelin is the 29-residue GRF(1-29) fragment. Tesamorelin is based on the full 44-residue GHRH sequence and carries a trans-3-hexenoyl cap on its N-terminus that stabilizes it against degradation.

What does the hexenoyl group on tesamorelin do?

It caps the N-terminus, a site vulnerable to enzymatic breakdown. Acylating it is the structural strategy that gives tesamorelin its stability, distinct from CJC-1295's substitutions or DAC linker.

Is tesamorelin a GHRH analog or a secretagogue?

A GHRH analog — it acts on the GHRH receptor, not the ghrelin (GHS) receptor used by ipamorelin and the GHRPs.


View Tesamorelin in the catalog →Certificates of analysis
Related research
SermorelinCJC-1295 (no DAC)CJC-1295 with DACIpamorelinCJC-1295 / Ipamorelin
Reference

This monograph is a research-use reference. It describes composition and the contexts in which the compound has been studied — it is not medical advice, a description of effects, or a recommendation for use. Sold strictly for laboratory and research use; not for human or animal consumption.