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Research Peptide
IGF-1 LR3 Research Kit
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99%+ purity
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Research
This listing supplies IGF-1 LR3 (Long R3 IGF-1) as a lyophilized reference material for in-vitro and preclinical laboratory work. IGF-1 LR3 is an 83-residue recombinant analog of human insulin-like growth factor 1, engineered with two structural modifications relative to the native 70-amino-acid protein: a 13-residue N-terminal extension and an arginine substitution at position 3 (in place of the native glutamic acid). These changes are the reason for the "Long" and "R3" in the name. The material is catalogued under CAS 946870-92-4 with the molecular formula C400H625N111O115S9, and each research lot is supplied at a documented purity of ≥98%. Because it is a folded, disulfide-bonded polypeptide rather than a short linear peptide, laboratories treat it as a recombinant protein standard when planning identity confirmation, reconstitution, and cold-chain storage.
The defining feature studied in the literature is that the position-3 substitution markedly lowers the analog's affinity for insulin-like growth factor binding proteins (IGFBPs). In native IGF-1 systems, IGFBPs sequester much of the free protein; the reduced binding of the R3 variant is the property that makes it a useful tool compound for researchers isolating receptor-level signaling from binding-protein modulation in cell-culture systems. All descriptions here concern the research substance itself and its documented study history — not outcomes in humans or animals. The body of work remains preliminary and ongoing, and nothing on this page constitutes medical advice.
Published investigations involving IGF-1 LR3 are predominantly in-vitro and cell-culture in nature, where the analog is frequently used as a supplement to serum-free culture media and as a probe of IGF-1 receptor (IGF-1R) signaling. Because of its diminished IGFBP affinity, it is a common reference agonist in studies dissecting downstream pathways such as PI3K/Akt and MAPK/ERK cascades under controlled conditions.
These references describe experimental laboratory work only. They are not medical claims, are not evidence of safety or efficacy in humans or animals, and should not be interpreted as guidance for any use outside a controlled research environment.
Each research lot is supplied as a lyophilized powder and characterized before release. Because IGF-1 LR3 is a larger, folded protein than a typical short peptide, identity and purity are established using orthogonal analytical methods so the material described on the Certificate of Analysis (COA) matches the sequence, mass, and disulfide-folded structure expected for the Long R3 analog. This dual-method approach separates purity (how much of the sample is the target protein) from identity (confirmation that the target is the correct molecule).
The COA accompanying each product is the definitive analytical record for that specific lot. Because purity and mass can vary slightly between production batches of a recombinant protein, researchers should reference the COA tied to the lot number received rather than generic specifications when documenting experimental inputs. Retaining the COA alongside experimental records supports reproducibility and traceability.
As a lyophilized recombinant protein, IGF-1 LR3 is sensitive to moisture and to repeated temperature cycling, both of which can compromise the folded, disulfide-bonded structure. Standard laboratory practice is to allow sealed vials to equilibrate to room temperature before opening to minimize condensation, and to reconstitute gently with an appropriate research-grade solvent under aseptic technique, avoiding vigorous vortexing that can shear or denature the protein. Aliquoting reconstituted stock into single-use portions limits freeze-thaw cycles that degrade protein integrity. Detailed temperature and stability windows for lyophilized, reconstituted, and working solutions appear in the storage table on this page.
IGF-1 LR3 is an 83-residue analog carrying two engineered changes relative to the native 70-amino-acid human IGF-1: a 13-residue N-terminal extension (the "Long" portion) and an arginine-for-glutamic-acid substitution at position 3 (the "R3" portion). The position-3 change is the property most studied in the literature because it substantially reduces affinity for IGF binding proteins (IGFBPs), which is why researchers use it as a tool compound to isolate receptor-level signaling from binding-protein effects in vitro.
It ships as a lyophilized (freeze-dried) powder in a sealed vial, sized by protein mass — here a 1 mg research kit. Lyophilization improves shelf stability for a recombinant protein and lets the researcher reconstitute with a solvent of their choice under aseptic conditions when preparing in-vitro experiments. It is supplied strictly as a laboratory reference material.
Purity is measured by reversed-phase HPLC and reported as a percentage of total peak area (≥98% for this material), while identity is confirmed by mass spectrometry (ESI-MS or MALDI-TOF) against the theoretical mass derived from the molecular formula C400H625N111O115S9. The lot-specific COA documents both values, plus appearance and net protein content, and is the authoritative analytical record for the exact material you receive.
Published work is predominantly in-vitro and cell-culture, where recombinant IGF-1 analogs are used as serum-free media supplements and as reference agonists in IGF-1 receptor signaling assays — including PI3K/Akt and MAPK/ERK pathway studies and comparative work isolating IGFBP-independent responses. This research is preliminary and ongoing, describes laboratory systems only, and does not establish any human or animal outcome.
This product is sold strictly for in-vitro research and laboratory use only. It is not intended for human or animal consumption, diagnostic purposes, or therapeutic application.
By purchasing this product, you confirm that you are a qualified researcher operating within an appropriate laboratory environment and will use this compound in accordance with all applicable local, state, and federal regulations.
Amino Science Labs assumes no liability for misuse of this product outside of its intended research application.
Allow the sealed vial to reach room temperature before opening to prevent condensation, reconstitute gently under aseptic technique with a research-grade solvent while avoiding vigorous vortexing that can shear the folded protein, and aliquot the stock to avoid repeated freeze-thaw cycles that degrade a disulfide-bonded recombinant protein. Follow the temperature and time windows in the storage table on this page for lyophilized, reconstituted, and working solutions.
No. This material is supplied strictly for in-vitro and laboratory research use by qualified researchers. It is not a drug, supplement, or food, is not intended for human or animal consumption or any diagnostic or therapeutic purpose, and nothing on this page constitutes medical advice.
