
Research evidence guide
IGF-1 LR3 research: distinguish the analog from native IGF-I.
A cited buyer guide to Long R3 IGF-I identity, IGF-binding-protein context, receptor and cell-assay evidence, model limits and the current non-clinical research listing.
Compare current prices and formats.
For qualified non-clinical research buyers. Not for human or veterinary use.

The analog name encodes a material difference
A protein-engineering paper describes Long R3 IGF-I as an N-terminally extended IGF-I analog and identifies an Arg substitution at position 3 of the IGF-I moiety.[1] That identity is not interchangeable with native IGF-I, des(1-3)IGF-I, tagged constructs or other IGF analogs. A shorthand listing also does not establish the complete sequence, terminal state, counterion, quantity basis or seller-lot identity.
Do not collapse receptor and binding-protein effects
IGF-binding proteins can change the extracellular availability of IGF ligands. One IGF1R-phosphorylation study found that IGFBP-3 inhibited signaling induced by several IGF ligands and analogs under its experimental conditions.[2] The paper also reported no direct IGFBP-3 interaction with IGF1R in its cross-linking experiment, supporting the need to distinguish ligand sequestration from receptor-level effects.
Cell background and conditioned medium matter
In postnatal rat lung fibroblasts, Long R3 IGF-I produced a different concentration-response from IGF-I in a cell-number assay; the investigators interpreted that comparison in the context of binding proteins present in conditioned medium.[3] The reported half-maximal values belong to that cell preparation, medium, exposure window and endpoint—not to all IGF1R assays.
Binding-protein resistance is not binding-protein independence
A porcine embryonic myoblast study describes Long R3 IGF-I as having very low affinity for IGF-binding proteins while retaining IGF-receptor binding.[4] In the same model, recombinant IGFBP-5 still suppressed the measured proliferation response, which the authors interpreted as evidence of an IGF-independent IGFBP-5 action. This illustrates why “reduced affinity” must not be rewritten as “unaffected in every system.”
Pathway readouts remain model-specific
Human intestinal smooth-muscle cells were used to examine DNA-synthesis responses and IGFBP production, with inhibitor experiments implicating MAP-kinase and PI3-kinase pathways in the measured system.[5] Separately, prostate cancer cell lines were used to study telomerase and Akt-associated readouts after IGF ligands and analogs.[6] Neither cell model establishes organism-level outcomes or the performance of a current seller lot.
Analytical identity cannot be inferred from a label
A forensic case report used immunoaffinity purification, intact-protein and peptide mass spectrometry, and an immunoassay to characterize a material as His-tagged Long R3 IGF-I.[7] The extra tag and linker made that material distinct from an untagged analog. The report is a useful identity warning: product names and immunoreactivity alone do not resolve sequence modifications or lot composition.
Procurement and assay checks for IGF-1 LR3
- Confirm the requested material is Long R3 IGF-I rather than native IGF-I, des(1-3)IGF-I, an antibody, a tagged construct or another analog.
- Record the supplied sequence, N-terminal extension, Arg substitution, terminal state, counterion or salt when stated, quantity basis and formulation.
- Match current lot documentation to the exact received material; literature and database records are not lot-specific evidence.
- Define receptor species and construct, cell background, receptor density, medium and serum conditions, exposure window, endpoint and controls.
- Record relevant IGF-binding proteins and conditioned-medium variables instead of assuming equal ligand availability across assays.
- Keep receptor phosphorylation, downstream signaling, proliferation, differentiation and organism-level observations in separate evidence tiers.
- Verify current seller price, availability, shipment eligibility and institutional receiving requirements before ordering.
Review the current research format
The card below uses current seller-catalog title, format, price and availability facts retrieved during generation. The literature above does not establish the identity, quality, purity, stability, performance or results of the seller product.
Sources
- Design and characterisation of long-R3-insulin-like growth factor-I muteins which show resistance to pepsin digestion — protein-engineering and digestion study.
- Effect of IGFBP-3 on IGF- and IGF-analogue-induced insulin-like growth factor-I receptor signalling — IGF1R phosphorylation and binding-protein study.
- Regulation of IGF-binding protein expression by growth factors and cytokines alters IGF-mediated proliferation of postnatal lung fibroblasts — rat fibroblast cell-number assay.
- Production of recombinant porcine IGFBP-5 and its effect on porcine embryonic myoblast cultures — myoblast proliferation and IGFBP study.
- Endogenous IGF-I regulates IGF binding protein production in human intestinal smooth muscle cells — cell and pathway-inhibitor study.
- Insulin-like growth factor I stimulates telomerase activity in prostate cancer cells — cancer-cell signaling study.
- Detection of His-tagged Long-R3-IGF-I in a black market product — analytical identity case report.