IGF-1 LR3 (Insulin-Like Growth Factor-1 Long R3) is a synthetic analogue of insulin-like growth factor-1, a peptide hormone that plays a key role in growth and cellular signalling pathways within the body.

The modified structure of IGF-1 LR3 includes an extended amino acid chain and a substitution at position three of the peptide sequence. These structural changes were developed in research environments to study how modifications to insulin-like growth factor molecules influence receptor interactions and biological signalling pathways.

Because insulin-like growth factor signalling is involved in processes such as cellular growth, tissue development, and metabolic regulation, IGF-1 LR3 has become a widely studied compound in research exploring endocrine and metabolic biology.

IGF-1 LR3: Quick Facts

Chemical Properties & Molecular Data

IGF-1 LR3 is a synthetic analogue of insulin-like growth factor-1. The peptide contains an additional 13 amino acids at the N-terminus compared with native IGF-1 and includes a substitution of arginine at position three.

These structural modifications were designed to alter receptor interaction and protein binding characteristics. In particular, IGF-1 LR3 has reduced affinity for certain binding proteins that normally regulate IGF-1 activity.

Because growth factor signalling plays an important role in cellular development and metabolism, modified IGF-1 analogues are widely studied in biochemical research exploring growth regulation pathways.

Mechanism of Action

In laboratory research, IGF-1 LR3 is studied for its interaction with IGF-1 receptor signalling pathways.

Research suggests the peptide may influence:

• insulin-like growth factor receptor signalling
• cellular growth regulation pathways
• protein synthesis mechanisms
• metabolic signalling pathways

Activation of the IGF-1 receptor triggers intracellular signalling cascades, including pathways involved in cell proliferation and metabolic regulation.

These mechanisms have made IGF-1 LR3 a subject of scientific investigation in studies exploring growth factor biology.

Areas of Scientific Research

IGF-1 LR3 has been studied in several areas of growth factor and metabolic research.

Common research topics include:

• cellular growth signalling pathways
• endocrine and metabolic biology
• protein synthesis regulation
• growth factor receptor signalling
• cellular proliferation studies

These research areas aim to better understand how growth factor signalling molecules influence cellular development and metabolic processes.

Reconstitution of IGF-1 LR3

IGF-1 LR3 is commonly supplied as a lyophilised peptide powder in order to preserve stability during storage and transport.

Before use in laboratory experiments, the peptide must be reconstituted into solution. This process typically involves introducing a sterile solvent into the vial to dissolve the peptide powder. In research settings, solvents such as bacteriostatic water or sterile laboratory water are commonly used.

The solvent is usually added slowly along the inside wall of the vial, allowing the powder to dissolve gradually. Gentle swirling may assist dissolution, while vigorous shaking is typically avoided to preserve peptide stability.

Researchers often determine the desired solution concentration before preparing peptide solutions. You can use our Peptide Calculator to estimate dilution ratios and final concentrations based on vial strength and solvent volume.

Storage of IGF1-LR3

Proper storage conditions are important for maintaining the stability and structural integrity of research peptides.

Lyophilised IGF-1 LR3 is typically stored in cool, dry laboratory conditions, often under refrigeration or freezing temperatures to preserve long-term stability.

Protecting peptide samples from moisture, light exposure, and repeated temperature fluctuations helps minimise degradation.

After reconstitution, peptide solutions are generally stored at lower temperatures and handled according to standard laboratory procedures to maintain stability during research studies.

References

1. Jones, J.I., & Clemmons, D.R. (1995). Insulin-like growth factors and their binding proteins.
   
2. Le Roith, D., et al. (2001). The insulin-like growth factor system and its biological functions.
   
3. Francis, G.L., et al. (1992). Recombinant analogues of insulin-like growth factor-I with altered receptor interactions.