Identity
an 83-amino-acid engineered analog of IGF-1 (native IGF-1 is 70 aa; ~9 kDa) with two changes — an arginine for glutamic acid at position 3 ("R3") and a 13-amino-acid N-terminal extension ("Long"). Together these cut its binding to IGF-binding proteins (IGFBPs) by ~100–1000×. Since ~98–99% of native IGF-1 is normally sequestered by IGFBPs (half-life ~10–20 min), evading them makes LR3 far more potent and long-lasting — half-life ~20–30 hours. At 83 aa it is a protein, above the "peptide" range, with three disulfide bonds — which is exactly why gray-market "IGF-1 LR3" is hard to fold, verify and trust.
Mechanism (as proposed)
IGF-1 LR3 binds the IGF-1 receptor (a receptor tyrosine kinase) → PI3K/Akt/mTOR (protein synthesis, survival, glucose uptake) and MAPK/ERK (proliferation) → in muscle, satellite-cell activation and new myonuclei/fibres. It also cross-reacts with the insulin receptor (lower affinity) → the hypoglycemia risk. The LR3 modifications let it slip past IGFBPs, so it stays free and active far longer than native IGF-1 — the same property that makes it potent is what makes its off-target and oncogenic risks harder to contain.