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Research Peptide
Tesamorelin Research Kit.
Fast shipping
Same-day dispatch
Third-party tested
U.S. accredited labs
99%+ purity
HPLC verified
44AA
SEQUENCE
Modified GHRH with trans-3-hexenoic acid
2010
FDA APPROVED
As Egrifta for lipodystrophy
15%
VAT REDUCTION
Visceral fat decrease in trials
150+
PUBLICATIONS
Clinical & preclinical studies
26min
HALF-LIFE
After subcutaneous injection
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on orders over $150
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Research
Tesamorelin is a synthetic analog of human growth-hormone-releasing hormone (GHRH), supplied here as a 10 mg lyophilized (freeze-dried) research peptide for in-vitro and preclinical laboratory work only. Structurally it is a stabilized 44-residue peptide corresponding to the full-length GHRH(1-44) sequence, distinguished from native GHRH by an N-terminal trans-3-hexenoyl (unsaturated fatty-acid) modification. This acylation is the defining feature of the molecule in the research literature: it hinders recognition by dipeptidyl peptidase-IV (DPP-IV), the enzyme that rapidly clips the N-terminus of unmodified GHRH, and thereby extends the peptide's measurable half-life in experimental systems. Investigators frequently reference the compound by its development code TH9507.
As a GHRH-receptor agonist, Tesamorelin is studied in laboratory settings as a tool compound for probing the somatotroph axis at the level of the pituitary GHRH receptor, rather than as a direct agonist of the growth-hormone receptor itself. This mechanistic position, upstream at a G-protein-coupled receptor, is part of why it appears in receptor-pharmacology and secretagogue research alongside shorter fragments such as GHRH(1-29). The material offered on this page is intended solely as a characterized reference compound for that kind of controlled, benchtop investigation.
The preclinical and in-vitro literature surrounding Tesamorelin centers on its interaction with the GHRH receptor and on the pharmacological consequences of its enzymatic stabilization. Reported research themes include the following, described strictly as observations in laboratory models rather than as outcomes in humans:
Because experimental parameters such as cell type, receptor construct, concentration range, and endpoint differ substantially between reports, cross-study generalization is not supported by the current data. This research is preliminary and ongoing, and the information here is educational only and not medical advice. Researchers reviewing this literature typically treat it as mechanistic and hypothesis-generating. Observations in isolated cells or animal models do not establish results in other biological systems, and this material is not a therapeutic product.
For a 44-residue peptide bearing an N-terminal acyl modification, analytical verification is central to reproducible results, because both sequence fidelity and correct modification must be confirmed. Research-grade Tesamorelin is typically assessed by reversed-phase high-performance liquid chromatography (RP-HPLC) to quantify chromatographic purity, usually reported as the percentage of the main peak. Mass spectrometry (commonly ESI-MS or MALDI-TOF) is used to confirm that the measured molecular mass matches the expected value for the modified 44-mer, verifying both identity and the presence of the trans-3-hexenoyl group rather than the unmodified backbone.
A lot-specific Certificate of Analysis (COA) documents these analyses. Researchers evaluating a batch generally review the reported HPLC purity value and chromatogram, the mass-spectrometry identity confirmation, and the net peptide content, since counter-ion (typically acetate) and residual water in a lyophilized powder mean the peptide mass in a given vial can differ from the gross fill weight. Confirming these figures against a current, lot-matched COA before use is standard practice and directly affects the accuracy of experimental concentrations.
Standard laboratory handling: the lyophilized powder is generally kept sealed, cold, and protected from light and moisture, with long-term storage of dry peptide commonly at -20 C or lower. Reconstituted solutions of a peptide of this length are less stable than the freeze-dried form and are typically kept cold and used within a limited, empirically confirmed window. These are material-handling notes for laboratory use only and do not imply any human or animal use.
Tesamorelin is a synthetic 44-amino-acid analog of growth-hormone-releasing hormone (GHRH), stabilized by an N-terminal trans-3-hexenoyl modification that resists DPP-IV cleavage. It is supplied as a 10 mg lyophilized powder for in-vitro and preclinical laboratory research as a GHRH-receptor agonist reference compound. It is a research chemical for laboratory use only, not a therapeutic product, and not for human or animal consumption.
It shares the full GHRH(1-44) sequence but carries an added trans-3-hexenoyl (unsaturated fatty-acid) group at the N-terminus. In research contexts this modification is significant because it hinders the enzyme DPP-IV from cleaving the N-terminal residues, which extends the peptide's measurable half-life relative to unmodified GHRH in experimental systems.
Laboratory studies characterize it as an agonist at the GHRH receptor, a G-protein-coupled receptor on pituitary somatotrophs, with downstream cyclic-AMP signaling used as an in-vitro endpoint. Additional research examines its enzymatic stability versus native GHRH. These are mechanistic, model-based observations from preliminary research and do not establish effects in humans.
Purity is typically assessed by reversed-phase HPLC and reported as a percentage of the main chromatographic peak, while mass spectrometry (ESI-MS or MALDI-TOF) confirms the molecular mass of the modified 44-mer, verifying both identity and the presence of the trans-3-hexenoyl modification. A lot-specific Certificate of Analysis (COA) records these results along with net peptide content.
This product is sold strictly for in-vitro research and laboratory use only. It is not intended for human or animal consumption, diagnostic purposes, or therapeutic application.
By purchasing this product, you confirm that you are a qualified researcher operating within an appropriate laboratory environment and will use this compound in accordance with all applicable local, state, and federal regulations.
Amino Science Labs assumes no liability for misuse of this product outside of its intended research application.
Related
A lyophilized peptide vial contains counter-ion (usually acetate) and residual water in addition to the peptide, so the net peptide mass can be lower than the gross fill weight. Reviewing the lot-matched COA for reported net peptide content and purity lets researchers calculate accurate stock concentrations, which is essential for reproducible in-vitro work.
As with other lyophilized research peptides, the dry powder is kept sealed and protected from light, heat, and moisture, with long-term storage commonly at -20 C or colder. Once reconstituted in an appropriate laboratory solvent, solutions are kept cold and used within a limited, empirically confirmed window. Handling follows standard institutional laboratory safety practice, and the material is for in-vitro research only.
