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IGF-1LR3 + GHRP-6 + Sermorelin (Blend)
IGF-1 LR3, GHRP-6, and Sermorelin are studied together for their potential to amplify anabolic signaling, stimulate natural growth hormone release, and support IGF-1 production through complementary mechanisms.
Quantity: 1
All peptides arrive in powdered form for stability
Third-Party Verified Purity
Each batch is tested and certified to meet or exceed 99% purity standards.
Made in the USA
Produced in United States WHO/GMP and ISO 9001:2015 certified facilities.
Rigorous Quality Control
Double-tested to ensure the highest quality for the most effective research.
What is IGF-1LR3 + GHRP-6 + Sermorelin (Blend)?
IGF-1 LR3 (Long Arg3 Insulin-Like Growth Factor-1) is a synthetic analog of human IGF-1 with a modified amino acid sequence that extends its half-life from minutes to over 20 hours, allowing for prolonged anabolic activity. GHRP-6 (Growth Hormone Releasing Peptide-6) is a synthetic hexapeptide that stimulates growth hormone (GH) release by activating ghrelin receptors, also known for its appetite-stimulating effects. Sermorelin is a 29–amino acid synthetic analog of growth hormone–releasing hormone (GHRH) that triggers natural GH release in a physiologic pulse pattern. In research settings, this combination is studied for potential synergistic effects on direct anabolic signaling, natural GH stimulation, and IGF-1 production.
Potential Benefits Shown in Studies
- Amplified Muscle Growth & Anabolic Signaling
- Prolonged IGF‑1 Activity
- Dual Pathway GH Stimulation
- Improved Recovery & Tissue Repair
- Enhanced Appetite & Nutrient Support
Mechanisms of Action
IGF-1 LR3 + GHRP-6 + Sermorelin may work together by:
- IGF-1 LR3: Binding directly to IGF-1 receptors in muscle, bone, and connective tissue to promote protein synthesis and cell growth
- GHRP-6: Activating ghrelin receptors (GHS-R1a) to trigger GH release from the pituitary while stimulating appetite
- Sermorelin: Binding to GHRH receptors to boost GH pulses, enhancing natural endocrine rhythms
- Increasing both circulating IGF-1 (via GH stimulation) and direct receptor activation (via IGF-1 LR3)
- Supporting muscle recovery, connective tissue repair, and improved nutrient utilization
- Enhancing collagen production and joint health in preclinical studies
Molecular Structure of Blend Components
IGF-1 LR3 Sequence
MFPAMPLSSL FVNGPRTLCG AELVDALQFV CGDRGFYFNK PTGYGSSSRR APQTGIVDEC CFRSCDLRRL EMYCAPLKPA KSA
Molecular Properties
Note: This version has a substitution of Arg (R) at position 3 and an extended N-terminal peptide chain.
IGF-1LR3 + GHRP-6 + Sermorelin (Blend) Research Highlights
IGF‑1 LR3 features an arginine substitution at position 3 and a 13-amino-acid N‑terminal extension, making it approximately three times more potent than native IGF‑1, with a significantly longer circulating half-life of ~20–30 hours.
Source: wikipedia
IGF‑1 LR3 is widely used in lab models for studying cell proliferation, metabolic regulation, stem cell maintenance, and tissue regeneration due to its long-lasting bioactivity.
Source: tydes
GHRP‑6, a synthetic hexapeptide, is known for its high potency in stimulating growth hormone (GH) secretion via the ghrelin receptor, distinguishing it from GHRH-based pathways.
Source: springer
In rat models, GHRP‑6 administered alongside doxorubicin prevented heart failure and multi-organ damage, boosting antioxidant defenses, preserving mitochondrial integrity, and reducing fibrosis.
Source: frontiers
Studies show that central administration of GHRP‑6 in rats triggers feeding behavior, activating hypothalamic and brainstem regions—even when animals had no access to food.
Source: academic
Sermorelin, a synthetic analog of GHRH (1–29), stimulates the pituitary gland to secrete growth hormone in natural, pulsatile patterns, maintaining feedback control and minimizing desensitization.
Source: pep-pedia
Originally approved in 1997 for treating childhood growth hormone deficiency, Sermorelin showed efficacy in reversing pediatric growth failure without the constant hormonal exposure of direct GH therapy.
Source: Wikipedia