GHRP-2 100mg — 45 Sprays

Scientific identity

GHRP-2 (CAS 158861-67-7), also designated Pralmorelin and investigational designation KP-102, is a synthetic hexapeptide growth hormone secretagogue. Its sequence is D-Ala–D-2-Nal–Ala–Trp–D-Phe–Lys–NH₂; molecular formula C₄₅H₅₅N₉O₆; molecular weight approximately 817.97 g/mol.

Compound class

Synthetic hexapeptide; growth hormone secretagogue (GHS); GHSR-1a agonist. Classified as a Research Use Only material and is not a drug, dietary supplement, food, or cosmetic.

Structural characteristics

GHRP-2 incorporates three D-amino acid residues — D-alanine at position 1, D-2-naphthylalanine (a synthetic aromatic residue) at position 2, and D-phenylalanine at position 5 — as well as a C-terminal primary amide. These features were introduced during synthetic GHS development to optimize receptor engagement and metabolic stability. The presence of D-amino acids and the unnatural 2-naphthylalanine residue means GHRP-2 does not correspond to any naturally occurring peptide sequence.

Primary molecular target

GHSR-1a (growth hormone secretagogue receptor type 1a) — a seven-transmembrane Gq/11-coupled GPCR expressed at highest density in pituitary somatotroph cells and hypothalamic nuclei relevant to growth hormone regulation.

Distinction from ghrelin

GHRP-2 and ghrelin share GHSR-1a as a pharmacological target but are chemically unrelated compounds. GHRP-2 should not be described as a ghrelin analogue in the structural sense.

Product content: 100mg per bottle; 45 sprays per bottle.

Physical form: Liquid research spray.

Purity: Research-grade.

Analytical documentation

A batch-specific Certificate of Analysis is available on the Longevia Research website, covering peptide identity, purity, and lot traceability.

Research-use classification. Research Use Only. Not approved for human or veterinary use. Not intended for administration to humans or animals.

Research background

Scientific interest in growth hormone-releasing peptides emerged in the late 1970s and early 1980s from pharmaceutical research programs — associated with Cyril Bowers and colleagues — aimed at developing synthetic ligands capable of stimulating growth hormone secretion through mechanisms distinct from growth hormone-releasing hormone (GHRH). GHRP-2 emerged from this program as a particularly potent synthetic hexapeptide GHS with well-characterized ability to stimulate growth hormone release in experimental systems. A significant aspect of GHRP-2's scientific legacy is its role in receptor identification: the cloning and characterization of GHSR by Howard and colleagues in 1996 used GHRP-2 and related ligands as pharmacological tools, establishing the existence of a previously unknown GPCR in the pituitary and hypothalamus with high affinity for synthetic GHS compounds. The subsequent identification of ghrelin in 1999 as the endogenous GHSR ligand completed this receptor biology research program, defining a broader physiological signaling axis in which GHRP-2 had served as a critical experimental tool.

Molecular target and mechanism

GHRP-2's mechanism of action is more clearly established at the receptor level than for many research compounds, reflecting decades of pharmacological characterization. GHRP-2 binds and activates GHSR-1a with high affinity and agonist efficacy, as established through radioligand binding assays, competition binding studies, and functional signaling assays in GHSR-expressing cell systems. GHSR-1a activation couples to Gq/11 proteins, activating phospholipase C (PLC), generating IP3 and DAG, and mobilizing intracellular calcium — a calcium signal in pituitary somatotroph cells proposed as a proximate mechanism for exocytosis of growth hormone secretory granules in experimental systems. In some animal model and human pharmacological studies, GHRP-2 has been observed to exhibit synergistic or additive effects on growth hormone secretion when combined with GHRH, suggesting potential second-messenger cross-talk between GHS and GHRH receptor systems at the pituitary level. Relative contributions of direct pituitary versus hypothalamic mechanisms, and the biological relevance of GHSR expression in peripheral tissues, remain areas of ongoing investigation.

Key research areas

Published research involving GHRP-2 spans GHSR-1a receptor pharmacology and ligand binding characterization; cell-based signaling studies examining intracellular calcium mobilization, IP3 generation, and downstream kinase activation in GHSR-transfected cell systems; rodent endocrine model studies characterizing growth hormone secretory responses including dose-response relationships and GHRH interaction; ex-vivo pituitary cell and tissue preparation studies examining GH secretion at the somatotroph level; and broader preclinical investigations of interactions with IGF-1 and appetite-related parameters given the metabolic relevance of ghrelin receptor biology. All preclinical findings are reported to provide scientific context and do not constitute evidence of human therapeutic efficacy or safety.

Human research and regulatory status

GHRP-2 has been studied in human subjects in clinical pharmacology and investigational settings — primarily examining acute growth hormone secretory responses following experimental administration, including investigation under the KP-102 designation in growth hormone deficiency diagnostic contexts. These studies established that GHRP-2 can stimulate measurable growth hormone secretion in controlled experimental conditions. The distinction between an experimentally observed pharmacodynamic effect and established therapeutic benefit is essential: acute hormone secretion responses in pharmacological studies do not automatically translate to beneficial outcomes in health, body composition, aging, or disease. GHRP-2 is not approved by the FDA, EMA, or any comparable regulatory authority as a drug or therapeutic agent for any human indication — including growth hormone deficiency, muscle wasting, obesity, or aging-associated conditions — and no marketing authorization exists for GHRP-2 as a pharmaceutical product in any jurisdiction.

Quality in synthetic GHS peptide research begins with the chemical identity of the compound. GHRP-2 is a structurally complex synthetic hexapeptide whose specific design features — three D-amino acid residues, a 2-naphthylalanine residue, and a C-terminal primary amide — are not only characteristic of the compound but functionally relevant to its receptor pharmacological activity. Analytical characterization of GHRP-2 research material must address these structural elements, as sequence errors, epimerization of D-amino acid residues, or the presence of synthetic byproducts can alter the compound's biological profile in experimental systems and compromise data reproducibility.

Peptide identity and sequence confirmation: The foundational quality requirement for any GHRP-2 research preparation is confirmation of the correct hexapeptide sequence: D-Ala–D-2-Nal–Ala–Trp–D-Phe–Lys–NH₂. This includes verification of D-amino acid configurations, the 2-naphthylalanine residue, and the C-terminal amide, all of which are structurally significant features that distinguish GHRP-2 from related but non-identical hexapeptide GHS compounds.

Mass spectrometric identity verification: Mass spectrometry — including electrospray ionization approaches — provides molecular weight determination at a precision capable of confirming the intact hexapeptide (MW ~817.97 g/mol, formula C₄₅H₅₅N₉O₆) and distinguishing the target compound from truncated sequences, deletion products, and synthesis-related impurities. For a structurally complex synthetic peptide such as GHRP-2, mass spectrometric confirmation is a central element of compound identity verification.

Chromatographic purity assessment: High-performance liquid chromatography (HPLC) provides complementary analytical characterization, enabling separation of GHRP-2 from co-eluting impurities and quantitative assessment of the purity profile at the batch level. Combined HPLC and mass spectrometric data provide the analytical foundation required for designing reproducible experiments with a well-defined research compound.

D-amino acid and stereochemical considerations: The presence of D-amino acid residues in GHRP-2 introduces stereochemical considerations that are relevant to analytical characterization. Epimerization of D-amino acids during synthesis or storage can yield closely related diastereomers with potentially different receptor pharmacological properties; analytical approaches that can distinguish stereoisomers — including chiral chromatography where appropriate — represent a quality consideration specific to D-amino-acid-containing research peptides.

Batch traceability: Linking experimental results to a defined, analytically characterized batch is a prerequisite for reproducible research and compliance with institutional requirements governing research chemical use. Batch-specific documentation supports research integrity and enables systematic review of experimental findings in relation to well-characterized material.

Longevia Research is committed to supplying research peptides that support rigorous scientific inquiry. Researchers are encouraged to review available analytical documentation for this product prior to incorporating it into laboratory workflows.

GHRP-2 100mg — 45 Sprays is supplied by Longevia Research strictly for research and laboratory use only. This product is not approved by the FDA or any global regulatory authority for human consumption, veterinary use, or therapeutic application. It is not a drug, dietary supplement, food, or cosmetic, and it is not manufactured, labeled, or sold as any of these under any applicable regulatory framework.

No claims made regarding GHRP-2 on this website are intended to diagnose, treat, cure, or prevent any disease or medical condition in humans or animals. The research findings summarized on this page arise from preclinical, biochemical, receptor pharmacology, and clinical pharmacology research contexts. These findings do not establish human therapeutic efficacy or safety for any application — including growth hormone deficiency, muscle growth, fat loss, athletic performance enhancement, anti-aging, or recovery — and they do not constitute regulatory approval, clinical validation, or authorization for personal or therapeutic use.

This product is sold exclusively to qualified researchers, laboratories, and scientific institutions for in-vitro and non-clinical laboratory research purposes. It is not intended for personal use, self-administration, resale for human consumption, or any application outside of a controlled research environment. Purchasers are responsible for ensuring that the acquisition, possession, handling, storage, use, and disposal of this compound are conducted in full compliance with all applicable local, state, federal, and international laws and institutional policies governing research chemicals.

By purchasing GHRP-2 from Longevia Research, the buyer confirms they are acquiring the product for legitimate scientific research purposes, agrees to handle and store it in accordance with applicable laboratory safety standards, and assumes full responsibility for compliance with all laws and regulations governing the purchase and use of research chemicals in their jurisdiction.