IGF-1 LR3 1mg Croissance musculaire

La forme longue durée de l'IGF-1. Analogue à 83 acides aminés dont l'extension N-terminale et la substitution Arg3 réduisent l'affinité aux protéines de transport : là où l'IGF-1 natif est neutralisé en quelques minutes, celui-ci reste actif des heures. Pureté HPLC ≥98 %, flacon de 1 mg. Produit destiné à la recherche.

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  • 1mg vialIncluded
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The vial alone cannot be used as is. One sealed vial of IGF-1 LR3 1mg, lyophilised, without individual labelling.

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Product information

IGF-1 LR3 (Long R3 Insulin-like Growth Factor 1) is a synthetic analogue of human IGF-1, with 83 amino acids against 70 for the native molecule. Two modifications set it apart: a 13-amino-acid N-terminal extension and the substitution of glutamic acid at position 3 with arginine (hence "R3").

Both changes target the same thing: affinity for the IGFBPs, the six binding proteins that sequester circulating IGF-1. Native IGF-1 is over 95% bound and its free plasma half-life is measured in minutes. The LR3 analogue binds them weakly and stays available far longer — that is the entire rationale for this research version.

This vial delivers 1 mg of IGF-1 LR3 at HPLC purity of at least 98%, lyophilised in type I borosilicate glass. For research use only.

Technical data
Science

01Mechanism of action

IGF-1 acts on the IGF-1R receptor, a transmembrane tyrosine kinase of the insulin receptor family. Binding triggers receptor autophosphorylation and then two main cascades: the PI3K/Akt/mTOR pathway, associated in the literature with protein synthesis and cell survival, and the MAPK/ERK pathway, associated with proliferation.

What sets LR3 apart is not mechanistic but pharmacokinetic. The IGFBPs, particularly IGFBP-3, form a ternary complex with native IGF-1 that extends its circulating presence while making it unavailable. By reducing that binding, the LR3 analogue increases the free fraction — the amount of molecule actually able to reach the receptor.

Worth noting, as it is a common confusion: reduced IGFBP affinity does not mean increased receptor affinity. LR3 binds IGF-1R with comparable, if slightly lower, affinity than native IGF-1.

Benchmark

Similar peptides

Against native IGF-1 (mecasermin). Same receptor, same cascade, but incomparable availability: native IGF-1 is over 95% sequestered by IGFBPs, LR3 largely escapes them. That is the only difference that matters in practice, and it is pharmacokinetic.

Against secretagogues (Ipamorelin, CJC-1295, Tesamorelin). The difference is one of level. Secretagogues act upstream: they stimulate the pituitary to release growth hormone, which then drives hepatic IGF-1 production. They therefore preserve physiological pulsatility and feedback loops. IGF-1 LR3 bypasses that chain and acts downstream, directly on the receptor. The two approaches are not interchangeable and are not documented in the same way.

Against MGF and PEG-MGF. MGF is a splice isoform of IGF-1, with a different E domain and local action; its pegylated form seeks to extend a naturally very short half-life. These are neighbouring but distinct molecules, with separate literatures.