Tesamorelin 10mg

Description

Tesamorelin 10mg – GHRH(1-44) Analog Research Peptide

Tesamorelin is the full 44-residue human growth hormone-releasing hormone, GHRH(1-44) amide, with one change: a trans-3-hexenoyl group on the N-terminal tyrosine. That single acyl group is the whole design. It is what separates tesamorelin from unmodified GRF(1-44) and from the shorter 29-residue fragment sermorelin, and it is why tesamorelin is studied as a model of how N-terminal modification protects a peptide hormone from enzymatic degradation.

Tesamorelin 10mg is supplied as lyophilised powder at 99%+ purity for in vitro and laboratory research. It is not approved for human or veterinary use.

Why the N-terminus matters

Native GHRH is short-lived in plasma. In 1986 Frohman and colleagues showed that plasma enzymes cut GHRH between its first two residues, Tyr1 and Ala2, and that the product, GHRH(3-44), is biologically inactive. The enzyme responsible is dipeptidyl peptidase-4 (DPP-4), which removes a dipeptide from any chain with alanine or proline in position 2.

Capping the N-terminal amine with a hexenoyl group blocks that cut without changing the rest of the sequence. Ferdinandi et al. (2007) measured the result directly, comparing the enzymatic stability of the modified peptide in plasma from several species and following its elimination kinetics. For researchers, tesamorelin is therefore a clean comparison pair with unmodified GRF(1-44): same receptor-binding sequence, different N-terminal protection.

The receptor it acts on

The GHRH receptor (GHRH-R) is a class B G-protein-coupled receptor, the same family as the receptors for glucagon, GLP-1, secretin and VIP. It was cloned from pituitary tissue in 1992. It couples mainly to G_s, so receptor activation is read out in vitro as a rise in intracellular cyclic AMP, the standard assay in cells engineered to express GHRH-R.

Class B receptors bind their ligands in two steps: the peptide’s C-terminal region docks onto the receptor’s large extracellular domain, and the N-terminal region then enters the transmembrane core to activate it. That is why the N-terminus of GHRH is both the part enzymes attack and the part that carries the activating signal, and why modifying it is a delicate trade-off.

Working with it in the lab

• Oxidation. Human GHRH carries a methionine at position 27. Oxidation to the sulfoxide adds 16 Da and is the most common degradation product in stored material. Mass spectrometry shows it as a +16 peak; HPLC usually resolves it as a slightly earlier-eluting shoulder.
• Deamidation. The asparagine at position 8 is a known deamidation site in GHRH peptides. Deamidation adds under 1 Da, so it is easy to miss by mass and is better tracked by chromatography.
• Size. At 5,136 g/mol, a single missing residue changes the mass by less than 3%. Purity for this molecule depends on chromatographic resolution more than on mass alone.
• Storage. Keep the lyophilised powder sealed, dry and cold. Once reconstituted, divide into single-use aliquots to avoid repeated freeze-thaw cycles, which speed both oxidation and aggregation. Our note on storage and stability of lyophilised peptides covers this in detail.

Questions researchers ask

How does tesamorelin differ from sermorelin? Sermorelin is GRF(1-29) amide, the shortest fragment of GHRH that keeps full receptor activity, with no N-terminal protection. Tesamorelin is the full 44-residue sequence plus the hexenoyl cap. They make a useful pair when studying how chain length and N-terminal protection each affect stability.

How does it differ from CJC-1295? CJC-1295 is built on the 29-residue fragment with four amino-acid substitutions, and in its DAC form a reactive group that binds albumin. Tesamorelin keeps the native sequence and relies on the N-terminal cap alone.

What identity check should the certificate show? An intact mass matching 5,136 g/mol, and an HPLC trace with the oxidised form resolved from the main peak.

Specifications

• 10 mg lyophilised peptide per vial
• Third-party HPLC for identity and purity, with the report published on this page
• Batch-level verification
• Dispatched from within Canada

Purity and quality assurance

ExoLabz products undergo independent third-party testing to verify peptide identity and purity, and results are published on this site. Researchers may run their own analytical verification. If validated testing confirms a purity discrepancy, ExoLabz provides a refund and testing reimbursement in line with company policy.

For research purposes only

Tesamorelin 10mg is supplied strictly for laboratory research and analytical use. It is not intended for human consumption, veterinary use, clinical research involving human subjects, therapeutic use or diagnostic applications. It has not been evaluated or approved by Health Canada, the U.S. Food and Drug Administration (FDA) or any other regulatory authority. By purchasing, the buyer confirms the material will be handled only by qualified professionals and used solely for lawful laboratory research.

Compound identity and specification

Identity data for Tesamorelin, published so the material can be checked against an independent record rather than taken on trust. The formula, mass and registry number below are verified against PubChem and can be looked up directly.

Analytical note — Tesamorelin. At 44 residues plus an N-terminal hexenoyl group this is the largest molecule in the catalogue, and the acyl group is the point: it is what distinguishes tesamorelin from unmodified GRF(1-44). On a 5,136 g/mol parent, a single-residue deletion is a mass shift of only about 1–3%, so purity here depends on chromatographic resolution more than on mass alone.

Identity references The molecular formula, molecular mass and CAS registry number above are taken from the PubChem record linked in the table, not from a supplier datasheet, so every figure can be checked against an independent source in one click. Sequences are given as reported in the peptide literature, in the one-letter or three-letter convention as appropriate, with any non-standard residue named in full. Where a compound exists in more than one form — a free peptide and a metal complex, a fragment and its parent protein, a modified and an unmodified analog — the form supplied is the one identified here, and the mass on the certificate of analysis is what distinguishes it.

Research Literature

Peer-reviewed studies involving this compound and its class. All findings listed are from in vitro, cell culture or animal models and are provided for scientific reference only. This product is supplied for laboratory research and is not approved for human consumption, clinical, or veterinary use.

• Ferdinandi ES, et al. Basic Clin Pharmacol Toxicol. 2007;100(1):49-58. In rats, dogs and pigs, measured enzymatic stability of the trans-3-hexenoyl modification, plasma elimination kinetics and plasma IGF-1 response. Source · PMID 17214611

Literature notes: Preclinical literature for this compound is limited; most published work reports clinical endpoints and is outside the scope of this reference list.

The third-party report for this material is published on this page, and every certificate we hold is collected on the certificates of analysis page.

Related Research Compounds

Browse more compounds in GHS, or view the full research peptide catalogue.

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