Skip to megamenu (after main content)
Meet us next:   BIO International Convention 2025 – 4 September  ●  ELRIG – Drug Discovery in Scotland 2025 – 17 September  ●  The Cell & Gene Meeting on the Mesa 2025 – 6-8 October (in person) & 9-10 October (virtual)  ●  ELRIG – Drug Discovery – 21-22 October  ●  more on our events calendar
Prices for NutriStem, NutriCoat, and NutriFreez products will increase effective 1st August. Lock in the current price by getting your order by 31st July.

Recombinant human IGF-2 protein

QK118

Brand: Qkine

Insulin-like Growth Factor 2 (IGF-2) is a growth factor that promotes cell proliferation, differentiation, and survival, particularly during fetal development. IGF-2 also regulates tissue growth and muscle regeneration.

Qkine human IGF-2 is a highly pure 7.5 kDa monomer, animal origin-free (AOF) and carrier-protein-free (CF). Qkine has optimised the IGF-2 manufacture process to produce a highly bioactive protein with excellent lot-to-lot consistency for enhanced experimental reproducibility.

Currency: 

Product name Catalog number Pack size Price Price (USD) Price (GBP) Price (EUR)
Recombinant human IGF-2 protein, 50 µg QK118-0050 50 µg (select above) $ 185.00 £ 140.00 € 164.00
Recombinant human IGF-2 protein, 100 µg QK118-0100 100 µg (select above) $ 280.00 £ 210.00 € 246.00
Recombinant human IGF-2 protein, 500 µg QK118-0500 500 µg (select above) $ 725.00 £ 540.00 € 631.00
Recombinant human IGF-2 protein, 1000 µg QK118-1000 1000 µg (select above) $ 1,050.00 £ 800.00 € 935.00

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
Insulin-like growth factor II, IGF2, IGF-II, Somatomedin-A, T3M-11-derived growth factor
Species reactivity

human

species similarity:
mouse – 91%
rat – 94%
porcine – 98%
bovine – 95%


Summary

  • High purity human IGF-2 protein (Uniprot: P01344)
  • 7.5 kDa
  • >98%, by SDS-PAGE quantitative densitometry
  • 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 sterile-filtered water at >50 µg/ml, add carrier protein if desired, prepare single use aliquots and store frozen at -20 °C (short-term) or -80 °C (long-term).
Handling and Storage FAQ

Featured applications

  • Cellular proliferation, migration and survival
  • iPSC and primary cell differentiation to muscle
  • Osteogenic differentiation

Bioactivity

Recombinant IGF-2 activity was determined using an SRE reporter assay on transfected MCF-7 cells. Cells were treated in triplicate with a serial dilution of IGF-2 for 4 hours. Firefly activity was measured and normalised to the control Renilla luciferase activity. Data from Qk118 lot 204687. EC50 = 58 ng/ml (7.8 nM)

Qk118-IGF-2-Datasheet-graph_-Qkine-protein

Purity

Recombinant IGF-2 migrates at approximately 7.5 kDa in reduced (R) and non-reduced (NR) conditions. No contaminating protein bands are present. The purified recombinant protein (3 µg) was resolved using 18% w/v SDS-PAGE in reduced (+β-mercaptoethanol, R) and non-reduced (NR) conditions and stained with Coomassie Brilliant Blue R250. Data from Qk118 lot #204687.

20241010-Qk118-IGF2-SDS-PAGE-1024x1024

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-2 is as biologically active as the comparable alternative supplier protein

Qk118-IGF-2-Peprotech-comparison

Qkine IGF-2 is as biologically active as the comparable alternative supplier protein. IGF-2 activity was determined using the serum response element (SRE) firefly luciferase reporter assay in transfected MCF-7 cells. Cells were treated in triplicate with a serial dilution of IGF-2 (Qk118, green) or alternative supplier IGF-2 (supplier B, black). Firefly luciferase activity was measured and normalized to the control Renilla luciferase activity. Data from Qk118 lot #204687.


Protein background

IGF-2, or Insulin-like Growth Factor 2, is a protein hormone that plays a crucial role in growth and development, particularly during fetal development. It is part of the insulin-like growth factor family, which includes IGF-1 and insulin. IGF-2 is a single-chain polypeptide consisting of 67 amino acids, with a molecular weight of 7.5 kDa. The protein’s three-dimensional structure is characterized by three alpha-helices stabilized by three disulfide bonds [1]. These disulfide bonds are formed between six conserved cysteine residues, which are critical for maintaining the protein’s tertiary structure and biological activity. The overall fold of IGF-2 is similar to that of insulin, reflecting their evolutionary relationship [2].

IGF-2 has numerous applications across various fields. In prenatal development, it is crucial for fetal growth and development, influencing organ size and body composition. It’s used as a marker in prenatal diagnostics to assess fetal growth and potential developmental issues [3]. In cancer research, IGF-2 has been implicated in various cancers, including colorectal, breast, and prostate cancer. It’s being studied as a potential biomarker for early cancer detection and as a target for cancer therapies. Given its role in glucose metabolism, IGF-2 is also being investigated in the context of metabolic disorders such as diabetes and obesity, with researchers exploring its potential in developing new treatments [4].

IGF-2 has tissue engineering and regenerative medicine applications, particularly in wound healing and tissue repair. IGF-2 has neuroprotective effects, suggesting potential applications in treating neurodegenerative disorders like Alzheimer’s disease. IGF-2 gene polymorphisms are used as genetic markers for selective breeding to improve meat quality and production efficiency [5]. Additionally, as a growth factor, IGF-2 is monitored in sports medicine to detect potential abuse for performance enhancement. The ongoing research into IGF-2’s structure and functions continues to open new avenues for applications in medicine, biotechnology, and agriculture, underlining its significance across multiple disciplines [6].

Background references

  1. Terasawa, H. et al. Solution structure of human insulin-like growth factor II; recognition sites for receptors and binding proteins. EMBO J. 13, 5590-5597 (1994). doi: 10.1002/j.1460-2075.1994.tb06896.x
  2. DeChiara, T. M., Efstratiadis, A. & Robertson, E. J. A growth-deficiency phenotype in heterozygous mice carrying an insulin-like growth factor II gene disrupted by targeting. Nature 345, 78-80 (1990). doi.org/10.1038/345078a0
  3. Livingstone, C. IGF2 and cancer. Endocr. Relat. Cancer 20, R321-R339 (2013). doi: 10.1530/ERC-13-0231
  4. Kido, Y. et al. Tissue-specific insulin resistance in mice with mutations in the insulin receptor, IRS-1, and IRS-2. J. Clin. Invest. 105, 199-205 (2000). doi: 10.1172/JCI7917
  5. Alberini, C. M. & Chen, D. Y. Memory enhancement: consolidation, reconsolidation and insulin-like growth factor 2. Trends Neurosci. 35, 274-283 (2012). doi: 10.1016/j.tins.2011.12.007
  6. Van Laere, A. S. et al. A regulatory mutation in IGF2 causes a major QTL effect on muscle growth in the pig. Nature 425, 832-836 (2003). doi: 10.1038/nature02064