Recombinant human IGF-2 protein

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).

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)

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.

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

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