Quick answer
What is IGF-1 LR3?
Built from index records dated 2026-10-09 to 2026-10-13 Compiled by an automated pipeline, checked by The Peptide Observer editorial desk How this site works
IGF-1 LR3 is not a peptide, grouped on this site under Growth factors and growth hormone-derived compounds, and the 12 research records kept here are 5 from studies in rats or mice and 7 that do not state what kind of study it is.
The literature search returned 46 records. This site keeps 12 of them, which is 26 per cent of what came back.
What it is
IGF-1 LR3 is indexed here despite not being a peptide, because the same research literature and the same searches cover it. This site puts it in the Growth factors and growth hormone-derived compounds group.
A modified insulin-like growth factor I; the retrieved records study it as an IGF-I analogue with reduced binding to IGF-binding proteins in myogenic cell and animal models.[1, 2]
Taken from the cited 2004 Journal of Cellular Physiology and 2005 Journal of Endocrinology titles, which examine it alongside IGF-binding proteins.
What kind of records
No public chemistry record was found under this name, so the entry describes a preparation, a protein or a mixture rather than one defined molecule.
That sentence is produced by counting, not by reading. What was counted: PubChem returned no compound record for this name, so the subject is a preparation, protein or mixture rather than a defined small molecule; identity fields are unsourced.
What this does not settle
- What it does in a body. Counting records is not reading them, and nothing here has been read in full.
- Whether it causes harm. No adverse-effect row was taken from any source for this entry.
- How long it lasts. No pharmacokinetics source was retrieved for this entry.
- What the other 34 retrieved records say. They are not in this index.
The longer explanation
Where this comes from
The records cited above, in full.
- Effect of recombinant porcine IGFBP-3 on IGF-I and long-R3-IGF-I-stimulated proliferation and differentiation of L6 myogenic cells. Journal of cellular physiology (2004). pmid:15254966
- Production of recombinant porcine IGF-binding protein-5 and its effect on proliferation of porcine embryonic myoblast cultures in the presence and absence of IGF-I and Long-R3-IGF-I. The Journal of endocrinology (2005). pmid:15817840