IGF-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.7kDa.
IGF-I is purified by proprietary chromatographic techniques.
The insulin-like growth factors (IGFs), including IGF1 and IGF2, are peptides that have crucial roles in the growth and development of mammals. IGF1 is particularly important for mediating the effects of growth hormone (GH). Research has shown that GH doesn't directly promote sulfate incorporation into cartilage. Instead, it acts through a serum factor originally called 'sulfation factor' and later renamed 'somatomedin' (Daughaday et al., 1972). This discovery led to the identification of three main somatomedins: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
Recombinant Rat IGF-1, produced in E. coli, is a single-chain polypeptide consisting of 70 amino acids. It is non-glycosylated and has a molecular weight of 7.7 kDa. The purification process of IGF-I involves proprietary chromatographic techniques.
IGF-1 is synthesized as a precursor protein that undergoes proteolytic processing to generate the mature form. In rats, IGF-1 is produced as four precursor isoforms with alternate N- and C-terminal propeptides . The mature IGF-1 protein consists of 70 amino acids and has a molecular mass of approximately 7.6 kDa . Recombinant IGF-1 is typically produced in Escherichia coli (E. coli) and purified using chromatographic techniques .
IGF-1 is a key regulator of growth and development. It promotes cell proliferation and differentiation, particularly in muscle, bone, and cartilage tissues. IGF-1 also has significant effects on metabolism, including enhancing protein synthesis and glucose uptake. It plays a role in the regulation of apoptosis, thereby contributing to cell survival .
IGF-1 is expressed in various tissues, with the highest levels found in the liver. It is also produced in other tissues, including muscle, bone, and cartilage, where it acts in an autocrine or paracrine manner. The expression of IGF-1 is regulated by several factors, including nutritional status, hormonal signals, and developmental stage .
Recombinant rat IGF-1 is produced using recombinant DNA technology. The gene encoding rat IGF-1 is inserted into an expression vector, which is then introduced into E. coli cells. The bacteria are cultured, and the recombinant protein is expressed and purified. Recombinant IGF-1 is used in various research applications, including studies on cell growth, metabolism, and cancer .
Recombinant IGF-1 is widely used in scientific research to study its effects on cell proliferation, differentiation, and survival. It is also used to investigate the mechanisms underlying growth and development, as well as its role in various diseases, including cancer and metabolic disorders. Additionally, IGF-1 is used in cell culture systems to promote the growth and maintenance of cells .