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15N-IGF-1, Uniformly Labeled, Human, Recombinant

Sequence: GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA

           
Product Catalog # SizePrice (USD) Quantity
$400.00
$2,000.00
$6,000.00
Synonym: 15N Stable Isotope Labeled Insulin-Like Growth Factor I; 15N-IGF-I; 15N-IGFI; 15N-IGF1; 15N-IGF-IA; 15N-Somatomedin C; 15N-Mechano Growth Factor; 15N-rhIGF-I
Unlabeled CAS #: 67763-96-6
UniProt ID: P05019
Source: E. coli
Molecular Formula: C331H518(15N)94O101S7
Molecular Weight: 7748.7
Uniformly 15N isotope-labeled human insulin-like growth factor-1 (IGF-1) is a valuable stable isotope-enriched recombinant protein widely used in structural biology, nuclear magnetic resonance (NMR) spectroscopy, and protein interaction studies. Human IGF-1 is a 70-amino acid peptide hormone that regulates cell growth, proliferation, differentiation, and survival through activation of the insulin-like growth factor-1 receptor (IGF-1R). Uniform incorporation of the stable 15N isotope enables high-resolution multidimensional NMR experiments without altering the native biological properties of the protein. As a result, uniformly 15N-labeled IGF-1 has become an indispensable research tool for investigating protein structure, receptor recognition, ligand binding, and therapeutic development in oncology, endocrinology, and regenerative medicine.
1. Introduction
Insulin-like growth factor-1 (IGF-1) is a highly conserved growth factor that shares significant structural homology with insulin. Produced primarily by the liver in response to growth hormone stimulation, IGF-1 plays a critical role in regulating normal growth, tissue repair, metabolism, and neuronal development.
Human IGF-1 consists of 70 amino acids stabilized by three intramolecular disulfide bonds, which are essential for maintaining its native tertiary structure and biological activity. Binding of IGF-1 to the IGF-1 receptor activates intracellular signaling pathways, including the PI3K/Akt and MAPK/ERK cascades, which regulate cell proliferation, apoptosis, and protein synthesis.
Because dysregulation of IGF-1 signaling is implicated in cancer, diabetes, cardiovascular disease, and neurodegenerative disorders, IGF-1 remains an important target for both fundamental research and drug discovery.
2. Importance of 15N Isotope Labeling
Uniform incorporation of 15N throughout the IGF-1 molecule provides numerous advantages for structural and biophysical studies:
• Enables high-resolution 1H-15N HSQC NMR spectroscopy.
• Facilitates complete backbone resonance assignment.
• Allows residue-specific analysis of protein folding and conformational dynamics.
• Supports investigation of receptor recognition and ligand-binding interfaces.
• Enables studies of interactions with IGF-binding proteins (IGFBPs), antibodies, and therapeutic molecules.
• Provides a stable, non-radioactive isotopic label without significantly affecting protein structure or biological activity.
These features make uniformly 15N-labeled IGF-1 particularly valuable for detailed mechanistic studies at atomic resolution.
3. Structural Characteristics
Human IGF-1 adopts a compact, well-defined three-dimensional structure stabilized by three conserved disulfide bonds. Unlike intrinsically disordered proteins, IGF-1 possesses a folded architecture that closely resembles insulin while containing unique structural elements responsible for receptor specificity.
Major structural features include:
• B-domain: contributes to receptor binding and structural stability.
• C-domain: influences receptor affinity and biological activity.
• A-domain: participates in receptor activation and stabilization.
• D-domain: involved in interactions with IGF-binding proteins and modulation of signaling.
Uniform 15N labeling enables residue-specific characterization of these domains and their conformational changes upon ligand or receptor binding.
4. Major Research Applications
4.1 Protein Structure Determination
Uniformly 15N-labeled IGF-1 is widely used for:
• Solution-state NMR spectroscopy
• Backbone resonance assignment
• Structural refinement
• Protein dynamics measurements
• Hydrogen–deuterium exchange studies
These experiments provide detailed insight into the molecular architecture and flexibility of IGF-1.
4.2 Receptor Binding Studies
The labeled protein facilitates investigation of interactions with:
• IGF-1 receptor (IGF-1R)
• Insulin receptor isoform A (IR-A)
• Hybrid IGF-1R/IR receptors
• Receptor extracellular domains
NMR chemical shift perturbation experiments enable identification of binding interfaces and conformational changes associated with receptor activation.
4.3 IGF-Binding Protein (IGFBP) Research
Approximately 99% of circulating IGF-1 is bound to IGF-binding proteins (IGFBPs), which regulate its stability, distribution, and biological activity.
Uniformly 15N-labeled IGF-1 supports structural studies of interactions with:
• IGFBP-1
• IGFBP-2
• IGFBP-3
• IGFBP-4
• IGFBP-5
• IGFBP-6
These investigations help elucidate mechanisms governing IGF-1 bioavailability and signaling.
4.4 Drug Discovery and Therapeutic Development
Uniformly 15N-labeled IGF-1 is an important reagent for evaluating:
• IGF-1R inhibitors
• Therapeutic antibodies
• Engineered IGF-1 analogs
• Peptide therapeutics
• Small-molecule modulators of the IGF signaling pathway
Residue-specific NMR studies provide valuable information on ligand binding, mechanism of action, and protein conformational changes.
5. Future Perspectives
Uniformly 15N-labeled IGF-1 is expected to play an increasingly important role in:
• High-resolution studies of IGF-1 receptor activation
• Development of targeted anticancer therapeutics
• Characterization of engineered IGF-1 variants
• Investigation of IGF signaling in aging and neurodegenerative diseases
• Integration of NMR with cryo-electron microscopy and computational structural biology
These applications will continue to advance our understanding of IGF-1 biology and support the development of novel therapeutic strategies.
Uniformly 15N isotope-labeled human IGF-1 is a versatile and powerful research reagent for structural biology, NMR spectroscopy, and molecular pharmacology. By enabling residue-specific characterization of protein structure, dynamics, and interactions while preserving native biological function, it provides critical insights into IGF-1 signaling, receptor recognition, and therapeutic mechanisms. As research on growth factor biology and targeted therapies continues to expand, uniformly 15N-labeled IGF-1 will remain an essential tool for both fundamental studies and drug discovery.

For Research & Development use only. Not for testing and/or use on humans.

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