IGF-1 LR3 1mg research peptide lyophilised powder

IGF-1 LR3

1mg

83 amino acid IGF-1 analogue with extended half-life. IGF-1 receptor research.

£49.99In Stock

98.134% purity · Supplier-reported analysis · Batch UKPL-449 · View certificate

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  • Research use only. For in-vitro laboratory research. Not for use in humans or animals, or in food, drugs or diagnostics. Not evaluated by the MHRA or FDA. The buyer is responsible for handling and regulatory compliance.

Bulk Pricing

Counted across your basket, any mix of products.

Vials in basketDiscountPer vial
1None£49.99
3-45%£47.49save £2.50
5-98%£45.99save £4.00
10-5012%£43.99save £6.00
Don't Forget

Bacteriostatic Water 10ml

Required to reconstitute lyophilised peptides.

£4.99

What is IGF-1 LR3?

IGF-1 LR3 (Long R3 IGF-1) is an 83 amino acid analogue of human insulin-like growth factor 1, supplied as a 1mg lyophilised powder. An Arg3 substitution and a 13 residue N-terminal extension cut its binding to IGF binding proteins about 1000-fold. That makes it a standard reagent for IGF-1 receptor research and serum-free cell culture.

Full description

The literature writes it as Long-[Arg3]-IGF-I or LR3IGF-I. It is native 70 residue IGF-I with two changes: arginine replaces glutamate at position 3, and a 13 residue extension, MFPAMPLLSLFVN, sits on the N-terminus. The extension is the first 11 residues of methionyl porcine growth hormone plus Val-Asn. It is left over from the fusion used to express the protein in Escherichia coli (Francis et al., J Mol Endocrinol, 1992). Both changes sit in the region that IGF binding proteins contact.

IGF-1 LR3 Research Applications

  • Serum-free culture: LongR3 sustained the viability of two recombinant CHO cell lines better than insulin under production conditions (Morris and Schmid, 2000).
  • Receptor signalling: a reagent for type 1 IGF receptor activation and downstream PI3K and MAPK signalling.
  • Binding protein biology: separating IGFBP sequestration from receptor pharmacology, the comparison the analogue was built to make.
Study details

Published in-vivo work is confined to animal models. There are no human clinical trials of IGF-1 LR3.

IGF-1 LR3 vs Native IGF-1 and the IGF Binding Protein Problem

Native IGF-I does not circulate free. Most of it is held by IGF binding proteins, mainly IGFBP-3, which limit its access to the receptor. In any system containing serum or secreted IGFBPs, the concentration you add is not the concentration the receptor sees. Ballard et al. (Growth Regulation, 1993) found IGF-I binds IGFBP-3 with about 1000-fold higher affinity than LR3IGF-I. In L6 myoblasts, that gave LR3IGF-I 5 to 10-fold greater potency.

The gain depends on the binding proteins. In chicken embryo fibroblasts, which secrete no detectable IGFBPs, Long [Arg3]-IGF-I was less potent than IGF-I (Francis et al., 1992). The trade-off is that IGF-1 LR3 is a poor model of native IGF-I physiology. Use it for receptor pharmacology and serum-free culture, and native IGF-I to study the binding protein axis itself.

Research Overview

IGF-1 LR3, written in the primary literature as Long-[Arg3]-IGF-I or LR3IGF-I, is an 83 residue recombinant analogue of human insulin-like growth factor 1. It differs from the native 70 residue growth factor in two respects: glutamate at position 3 is replaced by arginine, and a hydrophobic 13 residue extension (MFPAMPLLSLFVN) is fused to the N-terminus. The analogue was characterised by Francis and colleagues in the Journal of Molecular Endocrinology in 1992. The extension is not a rationally designed pharmacophore, it is a residual fragment of the methionyl porcine growth hormone fusion partner used to express the protein in Escherichia coli, characterised in a companion paper in the same journal and year. Both modifications sit in the region that IGF binding proteins recognise, and the functional consequence is a large loss of IGFBP affinity while type 1 IGF receptor binding is largely preserved. Ballard and colleagues (Growth Regulation, 1993) reported that native IGF-I binds IGFBP-3 with approximately one thousand times the affinity of LR3IGF-I. Since the great majority of circulating IGF-I is normally sequestered in IGFBP complexes, an analogue that escapes that buffering behaves very differently in any system containing binding proteins, and that is the reason the IGF 1 LR3 variant exists as a reagent at all. The three disulfide bridges of the IGF-I core are retained, which is why the molecular formula carries nine sulfur atoms, six from cysteine and three from methionine. The best established application of this IGF 1 peptide is industrial rather than physiological: LONG R3 IGF-I is a standard growth factor supplement in serum-free CHO and HEK293 culture, where Morris and Schmid (Biotechnology Progress, 2000) compared it directly against insulin. Published in-vivo work is confined to rodent, pig and non-human primate models. There are no published human clinical trials of IGF-1 LR3, and it holds no marketing authorisation in any jurisdiction.

Product Specifications

IGF-1 LR3 · Technical Data
Molecular Formula
C₄₀₀H₆₂₅N₁₁₁O₁₁₅S₉
Molecular Weight
9112.0 g/mol (values between 9111 and 9118 are reported across sources)
CAS Number
946870-92-4
Sequence
83 residues, [Arg3]IGF-I(1-70) carrying a 13 residue N-terminal extension, MFPAMPLLSLFVN
Native IGF-I (comparison)
70 residues, approximately 7649 g/mol
Disulfide Bonds
3, the IGF-I core folding pattern is retained
Purity
98.134% by HPLC
Batch
UKPL-449
Storage
-20°C lyophilised, 2-8°C reconstituted
Appearance
White lyophilised powder
Form
Lyophilised powder

Certificate of Analysis

Supplier-reported analysis. Independent third-party verification pending.

Batch
UKPL-449
Purity
98.134%
Specification
≥98.0%
Method
HPLC-UV/MS
Tested
Mar 2026

Need the certificate for an earlier batch? Request an older CoA

Storage and Reconstitution

Store the sealed 1mg vial at -20°C. Three methionines, two of them in the N-terminal extension, make dilute solutions prone to oxidation, so minimise headspace air and keep solutions cold and dark. Freeze-thaw cycles promote aggregation in disulfide-bonded proteins more than in short peptides, so freeze single-use aliquots.

Vials are sold on their own, without bacteriostatic water for mixing or other supplies.

How to reconstitute and handle

IGF-1 LR3 is a folded 9.1 kDa protein with three disulfide bridges, so agitation is the main hazard. Let the vial reach room temperature, run bacteriostatic water slowly down the inside wall and swirl gently until clear. Never shake: shear and air-liquid interface exposure drive aggregation. Dilute working solutions lose material to untreated plastic and glass, so use low-binding labware and prepare dilutions just before use.

  • Allow the vial to reach room temperature before opening so condensation does not settle on the cake.
  • Treat this as a folded protein, not a short synthetic peptide. At roughly 9.1 kDa with three disulfide bridges, IGF-1 LR3 is vulnerable to shear and to air-liquid interface denaturation, which is why agitation is the single most common cause of a cloudy or aggregated preparation.
  • Expect surface adsorption losses at low concentration. Dilute working solutions of an 83 residue growth factor lose measurable material to untreated polypropylene and glass, so use low-binding labware and prepare dilutions immediately before use rather than storing them.
  • The sequence carries three methionine residues, two of them in the N-terminal extension, all oxidation-sensitive. Minimise headspace air, protect from light, and do not leave dilute solutions standing at room temperature.
  • Store the reconstituted solution at 2-8°C and prepare single-use aliquots at -20°C for longer holding. Avoid repeated freeze-thaw cycles, which promote aggregation in disulfide-bonded proteins.
  • Handle under aseptic conditions, swabbing the stopper of both vials with alcohol before each needle entry. The site reconstitution guide and reconstitution calculator cover the full aseptic workflow and dilution arithmetic.

For the full method, see the peptide reconstitution guide and the reconstitution calculator.

Research References

Published research on IGF-1 LR3 is indexed on PubMed. See our full UK buyer's guide for IGF-1 LR3 and UK buyer's guide for IGF-1 LR3 CoA.

IGF-1 LR3 Price (UK)

IGF-1 LR3 1mg is for sale at £49.99 per vial, supplied from stock in the UK with a published supplier batch certificate. UK delivery is £4.50 by Royal Mail Tracked 24, free over £69.

IGF-1 LR3 · Price per vial
VialPriceCost per mg
IGF-1 LR3 1mgThis page£49.99£49.99

Prices are in GBP per vial and match the basket. See the FAQ for delivery and payment options, and quality & testing for how each batch is checked.

Frequently Asked Questions

What is the difference between IGF-1 LR3 and IGF-1?

The difference is 13 extra residues on the N-terminus and one point substitution, Arg for Glu at position 3, giving 83 residues instead of 70 and around 9112 g/mol instead of roughly 7649. Functionally the difference that matters is binding protein affinity: both modifications fall in the region IGF binding proteins recognise, so IGF-1 LR3 binds IGFBP-3 far more weakly than native IGF-I while retaining high affinity at the type 1 IGF receptor. Any experiment run in medium containing serum or secreted IGFBPs will therefore behave differently with the two molecules, and molar calculations must state which one the mass refers to.

Is IGF 1 LR3 the same as Long R3 IGF-1 or LR3IGF-I?

Yes, IGF 1 LR3, IGF-1 LR3, Long R3 IGF-1, Long-[Arg3]-IGF-I and LR3IGF-I all refer to the same 83 residue analogue. The unhyphenated IGF 1 LR3 spelling is simply a common search variant. The literature usually writes it Long-[Arg3]-IGF-I, and biopharmaceutical suppliers market it under the trade style LONG R3 IGF-I as a cell culture supplement. Quoting CAS 946870-92-4 avoids ambiguity when sourcing reference material.

Why does IGF-1 LR3 bind IGF binding proteins so weakly?

Because both of its modifications sit in the part of the molecule that IGF binding proteins read. The N-terminal tripeptide region of IGF-I contributes directly to IGFBP contact, so extending the N-terminus by 13 hydrophobic residues and swapping the acidic Glu3 for basic Arg3 disrupts that interface while leaving the receptor-binding surface intact. Ballard and colleagues (Growth Regulation, 1993) put the affinity gap at roughly one thousand fold for IGFBP-3. Wilson and colleagues later reported that, unlike IGF-I, the Long R3 variant did not raise serum IGFBP-3 in adolescent monkeys, consistent with the same structural argument.

What is the half-life of IGF-1 LR3?

There is no published human pharmacokinetic half-life for IGF-1 LR3, because the compound has never been through a human trial. The multi-day and twenty-plus-hour figures circulated online are not traceable to any peer-reviewed human dataset and should be treated as unsourced. What the literature does support is a mechanistic argument rather than a number: because the analogue largely escapes IGFBP binding, its distribution and clearance in animal models differ from native IGF-I, and Ballard and colleagues examined exactly that comparison in 1993. Any half-life value used in a research design should come from the model system being used.

Has IGF-1 LR3 been studied in humans?

No. Published IGF-1 LR3 research is entirely preclinical, covering cell culture plus rat, pig and non-human primate models, including work on intestinal growth in rodents and on hypoglycaemic potency in pigs and marmosets. It is not an approved medicine in any jurisdiction and holds no marketing authorisation. It is also prohibited in sport, since the WADA Prohibited List covers insulin-like growth factor 1 and its analogues under section S2. Supplied strictly for laboratory research use, not for human or veterinary use.

What is IGF-1 LR3 studied for in the laboratory?

Its most established use is as a growth factor supplement in serum-free mammalian cell culture, where Morris and Schmid (Biotechnology Progress, 2000) compared LongR3 against insulin in CHO lines expressing recombinant proteins, and where it is widely used in place of insulin at far lower concentrations. Beyond bioprocessing, IGF-1 LR3 is used as a reagent for probing IGF-1 receptor signalling, PI3K and MAPK pathway activation, and the specific question of how much of native IGF-I biology is attributable to binding protein sequestration rather than to receptor pharmacology, which is precisely the comparison the analogue was built to make.

Where can I buy IGF-1 LR3 in the UK?

UK Peptide Lab sells IGF-1 LR3 1mg online as a lyophilised powder, dispatched from the UK. The current batch, UKPL-449, carries a certificate covering identity, HPLC purity, mass spectrometry and content, published with the supplier-reported label because the record names no independent laboratory. With an 83 residue protein the best place to confirm what you are buying is that mass spectrometry line. Orders placed before 3pm on a working day are dispatched the same day, with free UK delivery over £69.

What purity is your IGF-1 LR3 1mg?

Batch UKPL-449 tested at 98.134% purity by HPLC against a ≥98.0% specification. Mass spectrometry found [M+H]+ at 9113.0 m/z, matching the 9112.0 g/mol molecular weight, and content was 1.08mg against 1mg declared. The certificate is published in the certificate section so you can check it before ordering.

Is IGF 1 LR3 legal to buy in the UK?

IGF-1 LR3 holds no marketing authorisation in the UK or anywhere else. UK Peptide Lab supplies it only as a reference material for in-vitro research. It is not a medicine and not for human or veterinary use. Buyers must be 18 or over and confirm research-only use. This is background, not legal advice, so check the rules for your own institution.

What is the IGF 1 peptide difference between LR3 and des(1-3) IGF-1?

Both bind IGF binding proteins weakly, by opposite routes. des(1-3)IGF-I deletes the first three residues of IGF-I. IGF-1 LR3 keeps all 70, substitutes Arg3 and adds a 13 residue N-terminal extension. Francis et al. (1992) found Long [Arg3]-IGF-I and des(1-3)IGF-I were the two most potent analogues in cell lines that secrete IGFBPs.

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