Folding and binding
The study compared native and misfolded IGF analogues, including Long-[Arg3]IGF-I; isomer-specific results are not batch identity verification.
Milner et al., 1995 →Long Arg3 IGF-I analogue
IGF-1 LR3 is an extended IGF-I analogue with an Arg3 substitution. The cited study examines folding and binding of defined IGF-I analogues.

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In vitro · Study formulation · IGF analogue folding and cell-based assays
The study compared native and misfolded IGF analogues, including Long-[Arg3]IGF-I; isomer-specific results are not batch identity verification.
Milner et al., 1995 →Literature findings; refer to the model and formulation studied.
IGF-1 LR3 — long arg3 igf-i analogue. The literature identity must be matched to the documented chemical form and composition of the supplied material.
The Arg3 substitution and N-terminal extension were examined for oxidative folding and interactions with the IGF-I receptor and IGF-binding proteins. The work separates isomers with different disulfide bonds; their properties must not be presented as one result for any LR3 preparation.
IGF analogue folding and cell-based assays
The study compared native and misfolded IGF analogues, including Long-[Arg3]IGF-I; isomer-specific results are not batch identity verification.
Evidence concerns the studied material and model, not the supplied BLOPEP batch.
Milner SJ, Francis GL, Wallace JC, Magee BA, Ballard FJ · 1995 · The Biochemical journal
DOI: 10.1042/bj3080865Nominal variant content; analytical results belong to the documented batch.
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