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Tesamorelin & Ipamorelin blend is a research-use-only laboratory material that pairs two synthetic peptides in a single sealed vial of lyophilised powder.
One peptide acts at the growth hormone–releasing hormone receptor, the other at the ghrelin receptor. Laboratories order it for GH-axis pharmacology, receptor cross-talk work and pulsatility studies in preclinical models.
Quantity
$43.20
Tesamorelin + Ipamorelin Blend · 10mg/3mg
$43.20$86.40
For Research Use Only. Not for human consumption or therapeutic treatment.
Compound Class and Structure
Tesamorelin & Ipamorelin blend is a co-formulated preparation of two synthetic peptides supplied as a lyophilised powder in a sealed glass vial. Tesamorelin is a stabilised analogue of human growth hormone–releasing hormone, built on the 44-amino-acid GRF(1-44) amide sequence and carrying a trans-3-hexenoyl group at the N-terminus, a modification associated in the literature with slower enzymatic cleavage by dipeptidyl peptidase-4. Ipamorelin is a short pentapeptide growth hormone secretagogue (Aib-His-D-2-Nal-D-Phe-Lys-NH2) with C-terminal amidation and non-natural residues that confer resistance to exopeptidase trimming. The two molecules belong to separate structural and pharmacological families and are combined so that both receptor routes can be examined within a single experimental article.
Receptor Pharmacology and Signalling
Tesamorelin engages the GHRH receptor (GHRHR), a class B1 G protein-coupled receptor expressed on pituitary somatotrophs. Canonical coupling runs through Gs, adenylyl cyclase and cAMP accumulation, with downstream protein kinase A activity, CREB phosphorylation and Pit-1/POU1F1-associated transcriptional regulation of the GH1 locus. Ipamorelin is a selective agonist at the growth hormone secretagogue receptor (GHSR1a), a class A GPCR that signals principally through Gq/11, phospholipase C-beta, inositol trisphosphate generation and mobilisation of intracellular calcium; GHSR1a is also studied for constitutive activity and beta-arrestin recruitment. Because the two ligands converge on the same secretory cell population through distinct second-messenger cascades, the blend is a common tool article for examining pathway additivity, synergy, heterologous desensitisation and interaction with somatostatin tone.
Research Areas, Models and Endpoints
Investigators apply this material in recombinant systems such as HEK293 or CHO lines expressing GHRHR or GHSR1a, in primary pituitary cell culture, in perifusion preparations of dispersed somatotrophs, and in rodent and other preclinical models. Measured endpoints typically include cAMP accumulation, calcium flux kinetics, competition binding and receptor occupancy, beta-arrestin recruitment, receptor internalisation time-courses, and transcript or protein levels for GHRHR, GHSR and GH1. Whole-animal work commonly relies on serial sampling with deconvolution analysis of secretory profiles, quantifying pulse amplitude, interpulse interval and secretory mass, alongside circulating IGF-1 and IGFBP-3 as downstream indices and JAK2/STAT5 pathway markers in target tissue. Comparative and stability chemistry — mass spectrometry confirmation, chromatographic profiling and peptide mapping — is a further research use.
Storage and Laboratory Documentation
The lyophilised blend is documented for freezer storage, typically at or below −20°C for long-term inventory, with short-term refrigerated holding where laboratory records require it. Vials are kept sealed, protected from light, and maintained in a dry, desiccated environment, since peptide powders are hygroscopic and moisture uptake is a recognised source of variability. Repeated warming and cooling cycles should be avoided and recorded when they occur. Good practice is to log the lot number, receipt date, storage location and temperature monitoring alongside the corresponding certificate of analysis, so that analytical identity can be traced for any result set generated with that lot.
Compliance Statement
This material is sold strictly for laboratory research. It is not a medicine, not approved for therapeutic use, and not intended for human or veterinary consumption.

Tesamorelin & Ipamorelin blend is a laboratory reference material that places two synthetic peptides of different pharmacological classes into one lyophilised article.
The first component is an analogue of growth hormone–releasing hormone, a long-chain peptide whose N-terminal modification is associated with resistance to dipeptidyl peptidase-4 cleavage. The second is a short amidated pentapeptide secretagogue that behaves as a selective agonist at the ghrelin receptor.
Because the two molecules recruit separate receptor families — a class B1 GPCR and a class A GPCR — the blend gives investigators two independent stimulatory routes onto the same somatotroph population within a single experimental article. That makes it a practical tool for dual-pathway studies in cell culture, receptor-transfected lines and preclinical rodent work, where signalling convergence, additivity and feedback regulation are the objects of measurement rather than any physiological outcome.

Real Peptides supplies this blend as a research-grade material with supply-chain facts that laboratories can verify before a single experiment begins.
Supplied strictly as a research material, not for human or veterinary use.

Most growth hormone–axis research articles engage a single receptor family. A releasing-hormone analogue works through a class B1 receptor coupled to adenylyl cyclase and cAMP, while a secretagogue of the ghrelin-receptor class works through a class A receptor coupled to phospholipase C and calcium mobilisation. Studying either alone limits what can be resolved about convergence.
This blend is distinguished by holding both mechanism classes in one article, so cAMP and calcium arms can be probed side by side under identical culture or model conditions. That supports crossed designs — pathway additivity, heterologous desensitisation, somatostatin-tone interaction and pulse-profile deconvolution — that are difficult to run cleanly when two separate materials must be matched.
It also differs from non-selective secretagogue classes studied historically, which show broader pituitary hormone cross-reactivity; the pentapeptide component is characterised in the literature for receptor selectivity, giving a cleaner attribution of any measured signal.
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