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RESEARCH USE ONLY • NOT FOR HUMAN CONSUMPTION

GH Research

IGF-1 LR3 1mg

$85.00

IGF-1 LR3 1mg is an extended synthetic analogue of insulin-like growth factor 1 featuring an N-terminal extension and an amino acid substitution that modify interactions with IGF-binding proteins.

It is investigated in research involving IGF-1 receptor signaling, protein-binding interactions, cellular growth, and growth factor biology.

For laboratory research use only. Not for human or veterinary use.

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Description

IGF-1 LR3 Technical Overview

IGF-1 LR3, also known as Long R3 IGF-I, is a synthetic analogue of insulin-like growth factor 1 (IGF-1). Its molecular structure contains an extended N-terminal region and an arginine substitution at the position corresponding to the third residue of mature IGF-1.

These modifications alter interactions with certain insulin-like growth factor binding proteins (IGFBPs), making IGF-1 LR3 a research compound of interest in growth factor signaling and cellular biology.

Experimental investigations involving Long R3 IGF-I have examined receptor activation, protein-binding interactions, cellular proliferation, and growth factor responses in defined laboratory models.

Compound Specifications

PropertyValue
Compound NameIGF-1 LR3
Alternative NameLong R3 IGF-I
ClassificationModified IGF-1 analogue
Sequence Length83 amino acid residues
Structural Modifications13-residue N-terminal extension and Glu-to-Arg substitution
Primary Research ReceptorIGF-1R
Related ProteinsIGF-binding proteins
SourceSynthetic or recombinant preparation
Vial Content1mg
Research CategoryGrowth Factor Research

Complete sequence, molecular mass, disulfide connectivity, and production method should correspond to the specific Long R3 IGF-I preparation.

Storage and Handling

  • Follow the manufacturer’s recommended stability conditions.
  • Protect the compound from moisture and unnecessary light exposure.
  • Minimize temperature fluctuations and contamination.
  • Use appropriate procedures for disulfide-containing protein preparations.

Lyophilized Format

IGF-1 LR3 may be manufactured as a lyophilized research protein. The formulation and stability of the supplied preparation depend on production methods, excipients, and storage conditions.

Research Use Disclaimer

IGF-1 LR3 is an experimental research compound and is not FDA-approved for human therapeutic use. Not intended for human or veterinary administration.

Frequently Asked Questions

What Is IGF-1 LR3?

IGF-1 LR3 is a modified 83-amino-acid analogue of IGF-1 developed for research into growth factor signaling.

How Does IGF-1 LR3 Differ From IGF-1?

It contains an additional N-terminal sequence and an amino acid substitution that alter its interactions with IGF-binding proteins.

What Receptor Is Associated With IGF-1 LR3?

Its principal research receptor is IGF-1R.

Is IGF-1 LR3 the Same as IGF-DES?

No. IGF-DES is a truncated IGF-1 derivative, whereas IGF-1 LR3 is an extended and modified analogue.

Is IGF-1 LR3 FDA-Approved?

No. IGF-1 LR3 is not FDA-approved for therapeutic use.

Research Overview

Long R3 IGF-I has been used in laboratory research to investigate the effects of modified growth factor binding characteristics on cellular responses.

IGF-1 Receptor Signaling

Experimental studies investigate IGF-1R-associated signaling and cellular responses to growth factor exposure.

IGF-Binding Protein Research

The structural modifications of Long R3 IGF-I reduce its affinity for certain IGF-binding proteins, providing a model for studying growth factor availability.

Cellular Proliferation Research

Long R3 IGF-I has been studied in cultured-cell models examining proliferation and growth factor-dependent responses.

Protein Structure Research

Comparisons with native IGF-1 help characterize relationships between protein sequence, binding affinity, and experimental activity.

Research Applications

Research AreaIn Vitro Application
IGF-1R SignalingReceptor activation assays
IGFBP ResearchProtein binding measurements
Cellular GrowthGrowth factor response assays
Protein ChemistryModified IGF-1 characterization

References

  1. Francis GL, Ross M, Ballard FJ, et al. (1992). Novel Recombinant Fusion Protein Analogues of Insulin-Like Growth Factor (IGF)-I Indicate the Relative Importance of IGF-Binding Protein and Receptor Binding for Enhanced Biological Potency. Journal of Molecular Endocrinology. Publication information.

Certificate of Analysis (COA)

Available batch-specific documentation should identify the complete Long R3 IGF-I structure, purity, content, and relevant analytical characteristics.

Peptide Lives — peptidelives.com

Additional information

Weight100 g

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