Greater than 95.0% as determined by SDS-PAGE.
IGF1 R36Q Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of Approximately 7.7kDa.
The IGF1 R36Q is purified by proprietary chromatographic techniques.
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSQRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.
Insulin-Like Growth Factor-1 (IGF-1) is a peptide hormone that plays a crucial role in growth and development in mammals. It is structurally similar to insulin and is involved in cellular growth, differentiation, and survival. IGF-1 is produced primarily in the liver and is regulated by growth hormone (GH). The mutant R36Q variant of IGF-1 is a specific alteration where the arginine ® at position 36 is replaced by glutamine (Q). This mutation can affect the biological activity and binding properties of IGF-1.
IGF-1 mediates many of the growth-promoting effects of GH. It is involved in various physiological processes, including:
Recombinant human IGF-1 (rhIGF-1) is produced using genetic engineering techniques. The gene encoding IGF-1 is inserted into a suitable expression system, such as bacteria or yeast, which then produces the protein. The recombinant protein is purified and used for various research and therapeutic purposes.
The R36Q mutation in IGF-1 can alter its interaction with IGF-1 receptors and binding proteins. This mutation may affect the stability, affinity, and overall biological activity of the protein. Studies on the R36Q variant help in understanding the structure-function relationship of IGF-1 and its role in different physiological and pathological conditions.
Recombinant IGF-1, including the R36Q mutant, is used in various research applications: