IGF-1 LR3 1mg

Description

IGF 1 LR3 is a research grade synthetic analog of human insulin like growth factor 1 designed for enhanced activity and extended receptor interaction in controlled laboratory systems.

This 83 amino acid peptide differs from native IGF 1 through the replacement of glutamic acid with arginine at position three and the addition of a 13 amino acid extension at the amino terminal end. These structural modifications significantly reduce its interaction with insulin like growth factor binding proteins, commonly known as IGFBPs.

Reduced binding to IGFBPs allows IGF 1 LR3 to remain more available in experimental systems and supports prolonged interaction with the insulin like growth factor 1 receptor, commonly known as IGF 1R. This characteristic makes it a useful research tool for studies requiring sustained and consistent receptor activation.

Researchers use IGF 1 LR3 to investigate signaling pathways associated with IGF 1R activation, including the PI3K, Akt, mTOR and Ras, MAPK pathways. These signaling networks are widely studied for their involvement in cellular proliferation, differentiation, survival, protein synthesis and metabolic regulation.

IGF 1 LR3 may also be used in laboratory models examining receptor binding, concentration response relationships, intracellular signaling, gene expression and cellular adaptation following extended growth factor exposure.

Its modified molecular structure makes IGF 1 LR3 particularly useful for comparative studies involving native IGF 1, IGF binding proteins and other growth factor analogs.

Each vial from PEPTEX Labs is supplied as a research grade lyophilized peptide and accompanied by analytical documentation. Testing may include HPLC purity analysis, mass spectrometry identity verification, net content testing and endotoxin analysis, depending on the individual production batch.

This product is supplied exclusively for qualified laboratory research. It is not intended for human or veterinary use, clinical administration or therapeutic application.