Reduced IGFBP binding
N-terminal truncation drops IGFBP affinity vs native IGF-1.
CAS: 112603-35-7
A truncated analogue of insulin-like growth factor 1 missing the first three N-terminal residues, studied for IGF-1 receptor activation with reduced binding-protein sequestration, including neurotrophic activity in CNS models.

N-terminal truncation drops IGFBP affinity vs native IGF-1.
Characterized at hippocampal excitatory synapses via PI3K.
HPLC + MS verified per batch. CoA included.
IGF-1 DES is a 67-amino-acid truncated variant of native human IGF-1 in which the first three N-terminal residues (Gly-Pro-Glu) are absent. The truncation markedly reduces affinity for the IGF binding proteins (IGFBP-1 through 6), allowing the molecule to act on the IGF-1 receptor with less binding-protein sequestration than native IGF-1. Preclinical work has examined effects on AMPA-receptor-mediated synaptic potentiation in the CA1 region of rat hippocampus and PI3K/Akt-dependent neurotrophic signaling, distinct from LR3-style systemic anabolic studies.
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