Greater than 95.0% as determined by SDS-PAGE.
Insulin-Like Growth Factor- II Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 67 amino acids and having a molecular mass of 7.5k Dalton.
IGF-II is purified by proprietary chromatographic techniques.
The IGF-2 gene is an imprinted gene, meaning it is expressed only from the paternal allele. This epigenetic regulation is crucial for its function. Abnormalities in the imprinting of the IGF-2 gene are associated with several disorders, including Wilms tumor, Beckwith-Wiedemann syndrome, rhabdomyosarcoma, and Silver-Russell syndrome .
Recombinant human IGF-2 is produced using E. coli expression systems. The recombinant protein is typically purified to high levels of purity, often exceeding 97%, and is used in various research and therapeutic applications . The recombinant form retains the biological activity of the native protein and is used in studies involving cell proliferation, particularly in cancer research .
IGF-2 exerts its effects by binding to specific cell surface receptors, including the IGF-1 receptor and the insulin receptor. This binding activates intracellular signaling pathways that promote cell growth, differentiation, and survival. In particular, IGF-2 has been shown to stimulate cell proliferation in various cell types, including human breast cancer cells .
The role of IGF-2 in growth and development, as well as its involvement in various diseases, makes it a significant target for research. Understanding the regulation and function of IGF-2 can provide insights into developmental biology and the mechanisms underlying certain cancers and growth disorders .