Recombinant human/bovine/porcine IGF-1 LR3 protein
QK041
Brand: Qkine
Human insulin-like growth factor 1 long arginine 3 (IGF-1 LR3) protein is a synthetic analog of IGF-1. The substitutions include an arginine substitution and an N-terminal protein extension. Consequently, IGF-1 LR3 has improved biological potency and extended half-life. IGF-1 LR3 can be used for the consistent, reproducible maintenance of human pluripotent stem cells.
Qkine IGF-1 LR3 is a highly pure and bioactive 9 kDa protein monomer, animal origin-free (AOF) and carrier-protein free (CF).

Currency:
Product name | Catalog number | Pack size | Price | Price (USD) | Price (GBP) | Price (EUR) |
---|---|---|---|---|---|---|
Recombinant human/bovine/porcine IGF-1 LR3 protein, 100 µg | QK041-0100 | 100 µg | (select above) | $ 80.00 | £ 60.00 | € 71.00 |
Recombinant human/bovine/porcine IGF-1 LR3 protein, 500 µg | QK041-0500 | 500 µg | (select above) | $ 195.00 | £ 140.00 | € 164.00 |
Recombinant human/bovine/porcine IGF-1 LR3 protein, 1000 µg | QK041-1000 | 1000 µg | (select above) | $ 260.00 | £ 190.00 | € 222.00 |
Note: prices shown do not include shipping and handling charges.
Qkine company name and logo are the property of Qkine Ltd. UK.
Alternative protein names
Species reactivity
porcine (pig)
bovine (cow)
Frequently used together with:
Summary
- High purity human IGF-1 LR3 protein (Uniprot: P05019 for IGF-1 wild-type protein)
- >98%, by SDS-PAGE quantitative densitometry
- 9 kDa
- Expressed in E. coli.
- Animal origin-free (AOF) and carrier protein-free.
- Manufactured in Qkine's Cambridge, UK laboratories
- Lyophilized from acetonitrile, TFA
- Resuspend in water at >100 µg/ml, prepare single use aliquots, add carrier protein if desired and store frozen at -20°C or -80°C
Featured applications
- Maintenance of pluripotency in human iPSC
- Cell culture media optimisation and replacement of insulin in defined media
Bioactivity

IGF-1 LR3 activity is determined using the Promega serum response element luciferase reporter assay (*) in transfected MCF-7 cells. Cells are treated in triplicate with a serial dilution of IGF-1 LR3 for 4 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. EC50 = 1.3 nM (11.7 ng/mL). Data from Qk041 lot #104315. *Promega pGL4.33[luc2P/SRE/Hygro] #E1340
Purity

IGF-1 LR3 migrates as a single band at 10 kDa in non-reducing (NR) conditions and upon reduction (R). No contaminating protein bands are visible. Purified recombinant protein (3 µg) was resolved using 18% w/v SDS-PAGE in reduced (+β-mercaptothanol, R) and non-reduced (NR) conditions and stained with Coomassie Brilliant Blue R250. Data from Qk041 batch #104315.
Further quality assays
- Mass spectrometry: single species with expected mass
- Analytical reversed-phase: single sharp peak
- Endotoxin: <0.005 EU/μg protein (below level of detection)
- Recovery from stock vial >95%
Qkine IGF-1 LR3 is stable and bioactive in conditioned media for 7 days
A
B
Stability and bioactivity of Qkine IGF-1 LR3 (Qk041). SDS-PAGE of recombinant IGF-1 LR3 (A), protein was not degraded when incubated in HEK293T conditioned media for 7 days. Bioactivity was determined using the IGF-1 LR3-responsive firefly luciferase reporter assay (B). Transfected HEK293T cells were treated in triplicate for 4 hours with a serial dilution of IGF-1 LR3 which had been pre-incubated in conditioned media for 2 or 7 days. Firefly luciferase activity was measured and normalised to the control Renilla luciferase activity.
Protein background
The insulin-like growth factors (IGFs) are a family of proteins with a similar structure to insulin. IGF-1 has an A and B chain connected by disulphide bonds, its similarity to insulin means it can bind with low affinity to the insulin receptor [1]. IGF-1 is a primary mediator of growth hormone (GH), with growth-promoting effects on most cells and tissues including skeletal muscle, cartilage, bone, liver, kidney, nerve, skin, hematopoietic, and lung [1]. IGF-1 exerts its biological effect through binding to the IGF1 receptor (IGF1R), its effect is modulated through interaction with a group of binding proteins (IGFBPs), which tend to inhibit the effect of IGF-1 [2]. Through IGF1R the Ras-MAPK and PI3 kinase signaling pathways are activated leading to increased cell proliferation and survival [2].
IGF-1 can be used to support maintenance of human embryonic stem cell (ESC) [3] and mesenchymal stem cell (MSC) cultures [3, 4].
Insulin-like growth factor long arginine 3 (IGF-1 LR3), is a widely used synthetic analog of IGF-1 with an arginine replacing glutamic acid at position 3 (arginine 3, R3), and an additional 13 amino acids at its N-terminus (long, L). IGF-1 LR3 retains the ability to bind IGF-1 and insulin receptors but has reduced binding affinity to insulin-like growth factor-binding proteins (IGFBPs). Consequently, IGF-1 LR3 has improved potency and metabolic stability [5].
Background references
- Z. Laron. Insulin-like growth factor 1 (IGF-1): a growth hormone. Mol Pathol. 2001 Oct;54(5):311-6. doi: 10.1136/mp.54.5.311
- H. Werner. The IGF1 Signaling Pathway: From Basic Concepts to Therapeutic Opportunities. International Journal of Molecular Sciences. 2023; 24(19):14882. doi.org/10.3390/ijms241914882
- L. Wang, T.C. Schulz, E. S. Sherrer, D. S. Dauphin, S. Shin, A. M. Nelson, C. B. Ware, M. Zhan, C. Z. Song, X. Chen, S. N. Brimble, A. McLean, M. J. Galeano, E. W. Uhl, K. A. D’Amour, J. D. Chesnut, M. S. Rao, C. A. Blau and A. J. Robins. Self-renewal of human embryonic stem cells requires insulin-like growth factor-1 receptor and ERBB2 receptor signaling. Blood 2007 Dec 1;110(12):4111-9. doi: 10.1182/blood-2007-03-082586
- A. Youssef, D. Aboalola and V. K. Han. The Roles of Insulin-Like Growth Factors in Mesenchymal Stem Cell Niche. Stem Cells Int. (2017) 9453108. doi: 10.1155/2017/9453108
- F. M. Tomas, S. E. Knowles, P. C. Owens, C. S. Chandler, G. L. Francis, L. C. Read and F. J. Ballard. Insulin-like growth factor-I (IGF-I) and especially IGF-I variants are anabolic in dexamethasone-treated rats. Biochem J. 1992 Feb 15:282, 91-7. doi: 10.1042/bj2820091