Luxara Labs Research Guide

IGF-1 LR3 Research Guide

IGF-1 LR3 is an 83-amino-acid analog of insulin-like growth factor 1 designed for controlled laboratory research involving IGF-1 receptor signaling, reduced binding-protein interaction, cellular growth pathways, metabolic signaling, and comparative analog studies. This guide separates established IGF-1 biology from the smaller body of evidence that directly evaluates IGF-1 LR3.

Updated July 29, 2026 IGF-1 Receptor Research 83 Amino Acids Research Use Only

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Direct Answer

IGF-1 LR3, also called Long R3 IGF-I, is an 83-amino-acid analog of human IGF-1. It contains a 13-amino-acid N-terminal extension and replaces the glutamic acid at position 3 with arginine. These modifications markedly reduce interaction with insulin-like growth factor-binding proteins while preserving activity at the IGF-1 receptor, making it useful in controlled studies of IGF1R signaling and related cellular pathways.

Research Overview

Key Takeaways

Modified IGF-1 Analog

IGF-1 LR3 is longer than native IGF-1 because it includes a 13-amino-acid N-terminal extension. It also carries an Arg substitution at position 3.

Reduced IGFBP Affinity

Its structural modifications substantially reduce binding to IGF-binding proteins. This can increase ligand availability in certain experimental systems, but the magnitude remains model and assay dependent.

IGF1R Signaling

Research commonly examines IGF-1 receptor activation and downstream PI3K-AKT and RAS-MAPK-ERK signaling associated with growth, survival, metabolism, and differentiation.

Not Interchangeable

Native IGF-1, IGF-1 LR3, and IGF-1 DES differ in length, binding-protein affinity, and experimental behavior. Results from one form should not automatically be assigned to another.

No Universal Half-Life

Commercial summaries often cite precise half-life figures, but experimental persistence varies with species, matrix, route, concentration, assay design, and binding-protein environment.

Evidence Boundaries Matter

Many research themes come from broader IGF-1 and IGF1R literature. Direct IGF-1 LR3 evidence is more limited and is concentrated in cell, tissue, livestock, and preclinical models.

Compound Definition

What Is IGF-1 LR3?

IGF-1 LR3 is a recombinant or synthetic research analog derived from the sequence framework of human insulin-like growth factor 1. Its design changes how the ligand interacts with IGF-binding proteins while retaining the ability to activate the type 1 IGF receptor.

Native human IGF-1 is a 70-amino-acid polypeptide. IGF-1 LR3 is 83 amino acids long because it adds a 13-amino-acid extension to the N-terminus. It also replaces the glutamic acid normally found at position 3 of IGF-1 with arginine. The name reflects these features: Long refers to the N-terminal extension, while R3 refers to arginine at position 3.

The main experimental consequence is reduced affinity for insulin-like growth factor-binding proteins, commonly abbreviated IGFBPs. IGFBPs normally regulate the distribution, sequestration, transport, and local availability of IGF ligands. By binding them poorly, IGF-1 LR3 can remain more available to interact with IGF1R in some cell-culture and tissue models.

Important distinction: reduced IGFBP affinity does not automatically establish a fixed whole-organism half-life or universal potency advantage. Experimental behavior changes with the model, receptor density, binding-protein profile, medium composition, exposure duration, and analytical method.

Molecular Comparison

IGF-1 LR3 Structure and Characteristics

IGF-1 LR3, native IGF-1, and IGF-1 DES share an IGF-1 sequence foundation, but their structural differences affect binding-protein interaction and experimental interpretation.

Feature	Native IGF-1	IGF-1 LR3	IGF-1 DES
Common name	Human IGF-1	Long R3 IGF-I, LR3 IGF-I	des(1-3)IGF-I
Amino-acid length	70 amino acids	83 amino acids	67 amino acids
Structural modification	Native mature IGF-1 sequence	13-amino-acid N-terminal extension plus Glu3 to Arg substitution	Deletion of the first three N-terminal residues of IGF-1
IGFBP interaction	Physiologic binding to multiple IGFBPs	Markedly reduced affinity in published binding assays	Reduced affinity relative to native IGF-1
IGF1R activity	Native receptor ligand	Retains IGF1R activity, with potency influenced by model conditions	Retains IGF1R activity, often studied where local IGFBP effects are important
Research interpretation	Best reference for normal IGF-1 physiology	Useful for examining IGF1R signaling with reduced IGFBP sequestration	Useful for studying a truncated analog with reduced binding-protein interaction
Half-life language	Depends on free versus bound ligand and biological context	No single universal value should be assigned across all models	No single universal value should be assigned across all models

Mechanistic Context

How IGF-1 LR3 Is Studied

The most established mechanistic framework comes from IGF1R biology. IGF-1 LR3 is commonly used as a ligand in models where researchers want to examine receptor signaling while limiting interference from IGF-binding proteins.

IGF-1 LR3 Research ligand with reduced IGFBP affinity

IGF1R Receptor autophosphorylation and adaptor recruitment

Downstream Networks PI3K-AKT and RAS-MAPK-ERK signaling

PI3K-AKT Signaling

IGF1R activation can recruit insulin receptor substrate proteins and stimulate phosphoinositide 3-kinase, AKT, mTOR, GSK3, and FOXO-related signaling. Researchers study this branch in relation to protein synthesis, cellular survival, nutrient sensing, metabolism, and growth regulation.

RAS-MAPK-ERK Signaling

IGF1R can also signal through SHC, GRB2, SOS, RAS, RAF, MEK, and ERK. This pathway is frequently examined in models of proliferation, differentiation, transcriptional regulation, and context-dependent cellular responses.

Evidence boundary: IGF1R pathway architecture is well established, but a pathway effect demonstrated with native IGF-1 is not automatically proof that IGF-1 LR3 produces the same magnitude, timing, or biological outcome in every model.

Scientific Context

Major IGF-1 LR3 Research Areas

These areas reflect a mixture of direct IGF-1 LR3 experiments and broader IGF-1 or IGF1R pathway research. Each section identifies the appropriate evidence context.

IGF-1 Receptor Signaling

IGF-1 LR3 is used to examine receptor phosphorylation, adaptor-protein recruitment, downstream kinase activity, feedback regulation, receptor internalization, and the influence of IGFBPs on ligand availability.

Evidence context: Direct LR3 studies plus extensive broader IGF1R literature.

Cell Proliferation Models

Published cell and embryo models have evaluated how low-IGFBP-affinity analogs influence DNA synthesis, cell-cycle entry, early cleavage, cell number, and growth under defined culture conditions.

Evidence context: Direct LR3 evidence exists, but results are strongly cell-type and medium dependent.

Protein Synthesis and Cellular Growth Signaling

The IGF1R-AKT-mTOR axis is widely studied in relation to translation initiation, ribosomal signaling, protein turnover, FOXO regulation, and cellular growth. LR3 may be selected where researchers want to reduce IGFBP-mediated sequestration.

Evidence context: Strong IGF-1 pathway evidence, with more limited direct LR3 evidence.

Skeletal Muscle Cell Research

Myoblast proliferation, differentiation, satellite-cell biology, myogenic signaling, and protein turnover are major IGF research themes. Direct LR3 studies in myogenic cell systems show that IGFBPs can alter proliferation and differentiation in different ways.

Evidence context: Direct cell-model studies and broad skeletal-muscle IGF1R literature.

Tissue Regeneration Models

IGF signaling is investigated in tissue growth, repair-associated cell behavior, extracellular matrix interaction, and regeneration-related pathways. A 2025 rat sciatic-nerve model incorporated controlled IGF-1 LR3 release into an experimental conduit, but this remains a specialized preclinical model and does not establish general regenerative effects.

Evidence context: Mostly broader IGF-1 biology, with emerging direct LR3 evidence in specialized animal and biomaterial models.

Metabolic Signaling Research

IGF1R and insulin-receptor networks overlap at several adaptor and kinase nodes. Researchers examine glucose handling, nutrient sensing, lipid metabolism, insulin signaling cross-talk, and feedback regulation under controlled conditions.

Evidence context: Broad IGF-1 metabolic literature with model-specific LR3 studies.

Glucose Uptake and Nutrient Signaling

Cell and tissue models may measure glucose transporters, glucose uptake, AKT activation, glycogen-related signaling, and interaction between IGF1R and insulin pathways. Findings cannot be generalized across tissues or translated into consumer outcomes.

Evidence context: Primarily IGF-1 and insulin-IGF system research.

Bone and Connective-Tissue Research

IGF-1 is studied in osteoblast, osteoclast, chondrocyte, tendon-cell, fibroblast, collagen, and matrix-regulation models. Local IGFBPs and mechanical conditions can materially change observed responses.

Evidence context: Strong broader IGF-system relevance, limited direct LR3-specific evidence.

Neuroscience and Neuronal-Survival Models

IGF1R signaling is studied in neuronal development, progenitor proliferation, synaptic biology, myelination, metabolism, and cell-survival pathways. In a 2025 male 5XFAD mouse study, long R3 IGF-1 altered aspects of cortical amyloid-plaque composition but did not preserve cognition or memory across the reported behavioral tests.

Evidence context: Broader IGF-1 neuroscience literature plus limited, mixed direct LR3 evidence in animal models.

Cancer-Cell and Abnormal-Proliferation Research

IGF1R signaling can support proliferation, survival, migration, metabolic adaptation, and resistance pathways in some cancer models. The role is not uniform across tumour types, and IGF1R may interact with integrins, insulin receptors, growth-factor receptors, stromal cells, and immune cells.

Evidence context: This is a major reason IGF-1 LR3 requires controlled research. It must not be presented as a cancer treatment or therapeutic agent.

Analog Comparison

IGF-1 LR3 vs Native IGF-1

The main practical distinction is not that one compound is universally stronger. It is that IGF-1 LR3 was engineered to interact much less strongly with IGF-binding proteins, which changes ligand availability in many experimental environments.

Research Question	Native IGF-1	IGF-1 LR3
Physiologic relevance	Better represents the endogenous mature ligand and its normal regulation by IGFBPs.	Represents an engineered analog with deliberately altered binding-protein behavior.
IGFBP-sensitive systems	Observed activity may be strongly moderated by the binding-protein environment.	Lower IGFBP affinity can increase apparent bioactivity in systems where binding proteins limit native IGF-1.
Receptor pathway work	Useful for studying native ligand-receptor regulation.	Useful for studying IGF1R signaling with less ligand sequestration by IGFBPs.
Data interpretation	Most appropriate for questions about normal IGF-1 physiology.	Most appropriate for analog-specific experiments and controlled ligand-availability questions.

IGF-1 LR3 vs IGF-1 DES

IGF-1 DES is a 67-amino-acid analog created by removing the first three residues from native IGF-1. IGF-1 LR3 moves in the opposite structural direction: it is longer than native IGF-1 and includes both an N-terminal extension and an Arg3 substitution. Both analogs show reduced interaction with IGFBPs, but they are structurally distinct and should not be treated as interchangeable.

Comparative potency claims require caution. A result depends on the specific binding protein, receptor expression, cell type, concentration, exposure window, medium, species, and assay endpoint. A compound that appears more active in one model may not behave the same way in another.

Practical research distinction: IGF-1 DES is useful for studying an N-terminally truncated analog, while IGF-1 LR3 is useful for studying an extended Arg3 analog. The correct choice depends on the experimental question, not a generalized ranking.

Evidence Quality

Research Limitations and Scientific Uncertainty

IGF-1 LR3 is frequently described online with more certainty than the literature supports. A rigorous guide must identify where evidence is direct, indirect, model specific, or absent.

Direct Evidence Is Limited and Mixed

Many mechanistic claims are supported by native IGF-1 or IGF1R research rather than IGF-1 LR3 experiments. Direct studies can also be negative or context dependent. For example, a 2025 growth-restricted fetal-sheep study did not find improved fetal growth, while a 2025 male 5XFAD mouse study reported plaque remodeling without preserved cognition.

Models Are Not Equivalent

Cell culture, isolated tissue, livestock, rodent, embryo, and tumour models can produce different results because their receptor and IGFBP environments differ.

Concentration Changes Interpretation

Receptor occupancy, insulin-receptor cross-reactivity, feedback inhibition, and pathway duration may change as experimental concentration changes.

Time Matters

Short phosphorylation studies, multi-day proliferation assays, and long exposure models answer different questions and should not be blended into one conclusion.

Binding Proteins Are Active Regulators

IGFBPs can regulate ligand transport and availability, and some also have IGF-independent cellular effects. Reduced ligand affinity does not remove every IGFBP-related influence.

No Consumer Translation

Laboratory findings do not establish safety, efficacy, dosing, treatment value, performance outcomes, or suitability for human or animal administration.

Quality Interpretation

Purity, Identity, Quantity, and Laboratory Testing

A research material should not be evaluated by one purity percentage alone. Purity, identity, measured quantity, lot traceability, and sterility-related testing answer different questions.

HPLC Purity Estimates the proportion of the main chromatographic component relative to detectable components.

Mass Spectrometry Supports identity assessment by comparing observed mass-related data with the expected molecule.

Measured Quantity Addresses how much material was measured and is separate from chromatographic purity.

Sterility and Endotoxin Separate microbiological or contamination-related questions that are not answered by HPLC purity.

Analytical Question	Typical Method or Evidence	What It Does Not Establish Alone
How chromatographically pure is the sample?	HPLC or UPLC profile with reported purity percentage	Exact identity, measured vial quantity, sterility, endotoxin status, or experimental suitability
Does the observed mass support the expected molecule?	Mass spectrometry, often LC-MS or MALDI-based analysis	Complete sequence confirmation, purity across every impurity class, or microbiological quality
How much material is present?	Quantitative assay, gravimetric data, amino-acid analysis, or validated content method	Purity or identity by itself
Can the result be matched to the supplied lot?	Product name, strength, lot number, test date, and linked COA	That every future lot has the same result

View Luxara Lab ResultsReview available batch and lot-specific analytical resources. How to Read a COAUnderstand purity, identity, lot matching, and analytical methods. Peptide Purity StandardsPlace a 99%+ result within a wider quality framework.

Luxara quality context: IGF-1 LR3 is presented under Luxara Labs' 99%+ purity standard. Researchers should review current shop information and match any available analytical result to the exact lot rather than assuming that one report applies to every batch.

Material Integrity

Storage, Handling, and Stability

Peptide stability depends on temperature, moisture, light, container integrity, oxidation, adsorption, concentration, pH, handling frequency, and freeze-thaw exposure. IGF-1 LR3 should be handled according to documented laboratory procedures appropriate to the material and experiment.

Lyophilized Material

Generally more stable than material in solution.
Should be protected from moisture, heat, and unnecessary light exposure.
Temperature transitions should be controlled to reduce condensation risk.
Lot identity and storage history should remain documented.

Material in Solution

Usually requires more tightly controlled refrigerated handling.
Stability can depend on buffer composition, pH, concentration, container surface, and microbial control.
Repeated freeze-thaw cycles can increase degradation or aggregation risk.
Study-specific stability should be validated rather than assumed.

For a broader laboratory overview, read the Luxara Labs Peptide Storage, Handling and Stability Guide. This page intentionally does not provide reconstitution quantities, concentrations, administration procedures, or body-use instructions.

Canada Research Context

Canadian Research and Regulatory Context

Luxara Labs presents IGF-1 LR3 strictly as a laboratory research material. The product is not represented for human or animal administration, therapeutic use, diagnosis, disease treatment or prevention, cosmetic use, food use, or consumer performance applications.

Research-use positioning depends on more than a label. Public claims, product presentation, instructions, documentation, customer qualification, shipping, and the actual intended application all affect regulatory context. Researchers and purchasing organizations remain responsible for determining whether a material and proposed protocol fit their institutional requirements and applicable laws.

Read the Luxara Labs Peptide Research Use Regulations in Canada resource for a plain-English overview of research-use framing, documentation, labeling, and claim boundaries.

Luxara Labs IGF-1 LR3

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For qualified laboratory research only. Not for human or animal use.

Research Supply Standards

Why Researchers Source IGF-1 LR3 From Luxara Labs

Luxara Labs combines research-only product positioning with Canadian fulfillment, clear product specifications, public education, and a wider testing and transparency framework.

99%+ Purity Standard

IGF-1 LR3 is offered under Luxara Labs' 99%+ purity standard, with broader guidance explaining how purity should be interpreted alongside identity and lot traceability.

Third-Party Testing Framework

Luxara Labs publishes a dedicated lab-results resource for available batch-specific reports and explains how HPLC and mass spectrometry contribute different analytical information.

Transparent Research Resources

Researchers can review COA education, purity standards, methodology, storage guidance, transparency pages, and research-use compliance resources.

Canadian Fulfillment

IGF-1 LR3 ships from Ontario, supporting domestic Canadian fulfillment and direct access to Luxara Labs customer support.

Canada and USA Delivery

Luxara Labs lists typical delivery of 1 to 3 business days in Canada and 3 to 5 business days in the United States, subject to courier conditions.

Professional Research Support

Luxara Labs can assist with product, order, documentation-location, and shipping questions while maintaining research-only boundaries and avoiding body-use protocols.

Research Summary

IGF-1 LR3 Research Summary

IGF-1 LR3 is an 83-amino-acid analog of human IGF-1 containing a 13-amino-acid N-terminal extension and an arginine substitution at position 3. These modifications markedly reduce affinity for IGF-binding proteins while preserving signaling through the IGF-1 receptor.

The strongest established scientific context is IGF1R biology, including PI3K-AKT and RAS-MAPK-ERK signaling. These networks regulate cell growth, proliferation, survival, differentiation, protein turnover, and metabolic responses. Direct IGF-1 LR3 evidence exists in selected cell, embryo, muscle, livestock, and preclinical systems, but much of the broader discussion relies on native IGF-1 research.

IGF-1 LR3 should therefore be described as a laboratory tool for controlled analog and receptor-signaling research, not as a consumer product or a proven therapeutic, performance, regenerative, neurological, metabolic, or cancer-related intervention.

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Frequently Asked Questions

IGF-1 LR3 Research Questions

What is IGF-1 LR3?

IGF-1 LR3 is an 83-amino-acid analog of human insulin-like growth factor 1. It contains a 13-amino-acid N-terminal extension and replaces glutamic acid at position 3 with arginine. It is studied as a low-IGFBP-affinity ligand for IGF1R signaling research.

What does LR3 mean in IGF-1 LR3?

The name refers to two structural features. “Long” reflects the added 13-amino-acid N-terminal extension, and “R3” refers to arginine, represented by R, at position 3 instead of the glutamic acid found in native IGF-1.

How is IGF-1 LR3 different from native IGF-1?

Native IGF-1 contains 70 amino acids and normally interacts with IGF-binding proteins. IGF-1 LR3 contains 83 amino acids and has markedly reduced affinity for those binding proteins. This changes ligand availability in many laboratory systems while preserving activity at IGF1R.

What is the difference between IGF-1 LR3 and IGF-1 DES?

IGF-1 LR3 is an extended 83-amino-acid analog with an Arg3 substitution. IGF-1 DES is a shortened 67-amino-acid analog missing the first three residues of native IGF-1. Both have reduced IGFBP interaction, but their structures and experimental behavior are not identical.

What signaling pathways are associated with IGF-1 LR3 research?

Research commonly focuses on IGF1R activation and downstream PI3K-AKT-mTOR and RAS-MAPK-ERK signaling. These pathways are associated with cell growth, survival, proliferation, differentiation, protein turnover, and metabolic regulation. Most pathway architecture is established through broader IGF-1 research.

Why is IGF-1 LR3 studied in cell-growth models?

IGF1R regulates growth and survival pathways, and IGF-1 LR3 interacts weakly with IGF-binding proteins. Researchers may therefore use it to study receptor-driven responses where native IGF-1 would be more strongly sequestered by binding proteins in the experimental environment.

Does IGF-1 LR3 have a confirmed universal half-life?

No single half-life value should be applied across all research settings. Persistence varies with species, tissue, matrix, concentration, exposure method, binding-protein environment, clearance, and assay design. Precise commercial half-life claims often oversimplify the evidence.

What are the main limitations of IGF-1 LR3 research?

Direct compound-specific evidence is limited compared with the broader IGF-1 literature. Results vary by model, species, cell type, receptor expression, IGFBP profile, concentration, exposure duration, and endpoint. Laboratory findings do not establish safety, efficacy, or suitability for human or animal use.

How should IGF-1 LR3 be stored for laboratory research?

Lyophilized material is generally more stable than material in solution and should be protected from moisture, heat, and unnecessary light. Material in solution usually requires tighter refrigerated control. Researchers should follow lot-specific documentation and validated laboratory procedures.

Why are purity and identity testing both important?

HPLC purity estimates the proportion of the principal chromatographic component, while mass spectrometry provides identity-related evidence based on observed mass. Neither result alone confirms measured quantity, sterility, endotoxin status, or suitability for a specific experiment.

Where can researchers source IGF-1 LR3 in Canada?

Luxara Labs supplies IGF-1 LR3 1mg strictly for qualified laboratory research and ships from Ontario. Researchers can browse the Luxara shop, review current product information, consult the purity and lab-results resources, and confirm shipping and research-use details before ordering.

Is Luxara Labs IGF-1 LR3 intended for human or animal use?

No. Luxara Labs IGF-1 LR3 is sold strictly for laboratory research. It is not intended for human or animal use and is not represented for therapeutic, diagnostic, cosmetic, food, veterinary, disease-related, or consumer performance applications.

Scientific Sources

Research References

These sources support the structural, binding-protein, receptor-signaling, muscle, metabolic, neurological, and cancer-research context described in this guide. Direct IGF-1 LR3 studies are distinguished from broader IGF-1 and IGF1R references.

Francis GL, et al. 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. 1992;8:213-223. PubMed record.
Flint DJ, et al. Several insulin-like growth factor-I analogues and complexes of insulin-like growth factors-I and -II with insulin-like growth factor-binding protein-3 fail to mimic the effect of growth hormone upon lactation in the rat. Journal of Endocrinology. 1994;140:211-216. PubMed record.
Prelle K, et al. Insulin-like growth factor I (IGF-I) and long R(3)IGF-I differently affect development and messenger ribonucleic acid abundance for IGF-binding proteins and type I IGF receptors in in vitro produced bovine embryos. Endocrinology. 2001;142:1309-1316. PubMed record.
Tomas FM, et al. IGF-I variants which bind poorly to IGF-binding proteins show more potent and prolonged hypoglycaemic action than native IGF-I in pigs and marmoset monkeys. Journal of Endocrinology. 1997;155:377-386. PubMed record.
Xi G, et al. Effect of recombinant porcine IGFBP-3 on IGF-I and long-R3-IGF-I-stimulated proliferation and differentiation of L6 myogenic cells. Journal of Cellular Physiology. 2004. PubMed record.
White A, et al. Attenuated glucose-stimulated insulin secretion during an acute IGF-1 LR3 infusion into fetal sheep does not persist in isolated islets. Journal of Developmental Origins of Health and Disease. 2023;14:353-361. PubMed record.
White A, et al. IGF-1 LR3 does not promote growth in late-gestation growth-restricted fetal sheep. American Journal of Physiology-Endocrinology and Metabolism. 2025;328:E116-E125. PubMed record.
Engel MG, et al. Intranasal long R3 insulin-like growth factor-1 treatment promotes amyloid plaque remodeling in cerebral cortex but fails to preserve cognitive function in male 5XFAD mice. Journal of Alzheimer's Disease. 2025;103:113-126. PubMed record.
Yavuz E, et al. Revolutionary decellularized Alstroemeria stem-based nerve conduit integrated with GelMA and controlled IGF-1 LR3 release for enhanced rat sciatic nerve regeneration. International Journal of Biological Macromolecules. 2025;329:147888. PubMed record.
Yoshida T, Delafontaine P. Mechanisms of IGF-1-mediated regulation of skeletal muscle hypertrophy and atrophy. Cells. 2020. PubMed record.
Philippou A, et al. Type I insulin-like growth factor receptor signaling in skeletal muscle regeneration and hypertrophy. Journal of Musculoskeletal and Neuronal Interactions. 2007;7:208-218. PubMed record.
Kasprzak A. Insulin-Like Growth Factor 1 (IGF-1) Signaling in Glucose Metabolism in Colorectal Cancer. International Journal of Molecular Sciences. 2021;22:6434. PubMed record.
D'Ercole AJ, Ye P. Expanding the mind: insulin-like growth factor I and brain development. Endocrinology. 2008. PubMed record.
Bondy CA, Cheng CM. Signaling by insulin-like growth factor 1 in brain. European Journal of Pharmacology. 2004. PubMed record.
LeRoith D, Roberts CT Jr. The insulin-like growth factor system and cancer. Cancer Letters. 2003. PubMed record.
Galifi CA, Wood TL. Insulin-like growth factor-1 receptor crosstalk with integrins, cadherins, and the tumor microenvironment: sticking points in understanding IGF1R function in cancer. Endocrine-Related Cancer. 2023;30:e230031. PubMed record.
Conlon MA, et al. Long R3 insulin-like growth factor-I (IGF-I) infusion stimulates organ growth but reduces plasma IGF-I, IGF-II and IGF binding protein concentrations in the guinea pig. Journal of Endocrinology. 1995. PubMed record.
Ballard FJ, et al. Des(1-3)IGF-I: a truncated form of insulin-like growth factor-I. International Journal of Biochemistry and Cell Biology. 1996. PubMed record.

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