IGF1-LR3 1mg

Molecular Composition of IGF1-LR3 1mg

IGF1-LR3 is a synthetic analog of insulin-like growth factor 1 (IGF-1) that has garnered significant attention in research and clinical settings. Its molecular structure begins with a sequence of 83 amino acids, a modification that extends the half-life of the peptide compared to its natural counterpart. This elongation facilitates its sustained action within biological systems, allowing for prolonged efficacy in various applications, particularly in growth and developmental processes.

A key aspect of IGF1-LR3 is its amino acid modifications. The primary distinction from IGF-1 arises from the addition of a specific dibasic amino acid at the C-terminus. This alteration is crucial as it imparts enhanced binding affinity to the insulin-like growth factor receptor (IGF-1R), thereby amplifying its biological activity. Furthermore, the peptide has been altered at the Arginine residue in position 3, substituting it with a Leucine, which plays an essential role in its stability and biological function.

The purity level of IGF1-LR3 is typically reported at 99%, a parameter that is critical for researchers seeking reliable results. High purity ensures that any biological effect observed can be attributed to IGF1-LR3 alone, minimizing the risk of interference from contaminants. In addition to purity, the molecular weight of IGF1-LR3 is approximately 9 kDa, which allows for solubility in various solvents common in laboratory settings. Researchers have found IGF1-LR3 to be stable across a range of pH levels, contributing to its versatility in formulations and experimental setups, as it maintains its functional integrity under diverse conditions.

Understanding the molecular composition of IGF1-LR3 is paramount for its application in scientific research, as these characteristics directly influence its efficacy and reliability in experimental protocols.