LR3 IGF1 Human
Greater than 98.0% as determined by SDS-PAGE.
Description
Recombinant Human LR3 Insulin Like Growth Factor-1 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 83 amino acids and having a molecular mass of 9.1kDa.
Product Specs
The product is lyophilized from a 0.2µm filtered solution concentrated in 20mM PB, at a pH of 7.2.
The purity is determined to be greater than 98.0% using SDS-PAGE analysis.
Product Science Overview
LR3 IGF-1 differs from native IGF-1 in two significant ways:
- Amino Acid Substitution: The third amino acid in the sequence of IGF-1 is replaced with an arginine residue instead of the naturally occurring glutamic acid. This substitution is referred to as “arginine 3”.
- Extended N-Terminus: LR3 IGF-1 has an additional 13 amino acids at its N-terminus, resulting in a total of 83 amino acids compared to the 70 amino acids in native IGF-1 .
These modifications result in LR3 IGF-1 having a significantly reduced affinity for insulin-like growth factor-binding proteins (IGFBPs), which normally inhibit the biological activity of IGF-1. Consequently, LR3 IGF-1 exhibits enhanced metabolic stability and potency, making it approximately three times more potent than native IGF-1 .
LR3 IGF-1 retains the pharmacological activity of IGF-1 as an agonist of the IGF-1 receptor. This receptor is involved in various cellular processes, including cell growth, differentiation, and survival. The enhanced stability and potency of LR3 IGF-1 make it particularly useful in research settings where prolonged activity is required .
In addition to its research applications, LR3 IGF-1 is also used in the production of recombinant biopharmaceuticals. Its ability to support mammalian cell culture makes it an essential component in the large-scale manufacturing of these products .
LR3 IGF-1 is typically produced using recombinant DNA technology. The gene encoding the modified IGF-1 is inserted into a suitable expression system, such as Escherichia coli (E. coli). The bacteria are then cultured, and the recombinant protein is harvested and purified. This process ensures a high yield of LR3 IGF-1 with consistent quality and activity .
