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IGF-1 LR3, 1mg, lyophilized research peptide vial, Eppix Labs
Certificate of Analysis — 1mgCertificate of Analysis for IGF-1 LR3 1mg
Chemical StructureIGF-1 LR3 chemical structure
Amino Acid SequenceIGF-1 LR3 amino acid chain
Latest COA

IGF-1 LR3

Janoshik

Batch IGF1-CA-26A-01

Result2026-01-16
Added2026-08-02
Avg Purity98.587%
Avg Mass1.12 mg
Verify on Janoshik
In StockResearch Peptide
BatchIGF1-CA-26A-01

IGF-1 LR3

Long-Acting IGF-1 Analogue

IGF-1 LR3 is a long-acting analogue of insulin-like growth factor studied in laboratory settings for its role in cell growth signaling and protein synthesis pathways. Research often examines its interaction with IGF-1 receptors, as well as its influence on cellular proliferation, nutrient utilization, and anabolic signaling processes in controlled models.

$54.99USD
Purity VerifiedLab TestedSecure
Research Use Only

This product is intended strictly for laboratory research use within the United States. It is not approved by the FDA for the diagnosis, treatment, cure, or prevention of any disease. Not for human or veterinary use.

By purchasing, you confirm the material will be used solely for lawful research purposes in accordance with applicable U.S. federal, state, and local regulations.

IGF-1 LR3 is a synthetic analogue of insulin-like growth factor 1 (IGF-1) modified with an extended amino acid sequence to alter receptor interaction characteristics. It is developed for controlled laboratory research involving IGF-1 receptor signaling systems.

In scientific literature, IGF-1 LR3 is studied in experimental models examining IGF-1 receptor activation pathways, intracellular signaling cascades, and downstream cellular regulatory mechanisms under in vitro and preclinical research conditions.

Purity

Third-party tested for purity, identity, quantity.

Amino Acid Sequence
Amino acid chain diagram
Chemical Structure
Chemical structure diagram
Compound Properties
CAS Number123618-03-1
Molecular FormulaC71H119N17O19S
Molecular Weight1546.9 g/mol
PubChem CID5748425

Overview

IGF-1 LR3 is a modified form of IGF-1 engineered to alter binding characteristics and receptor interaction dynamics in experimental systems. Research has examined its interaction with IGF-1 receptor pathways and associated intracellular signaling frameworks within controlled laboratory environments.

Preclinical studies evaluate receptor-mediated signaling cascades, cellular growth-related pathways, and regulatory mechanisms under structured research conditions.

History

Insulin-like growth factor 1 (IGF-1) was identified as a key mediator in growth-related signaling pathways. Subsequent biochemical research led to the development of modified analogues such as IGF-1 LR3, designed to adjust receptor interaction properties for experimental study.

Research expanded into receptor-binding dynamics and intracellular pathway activation models within endocrine and cellular signaling frameworks.

Key Research Areas

Laboratory investigations into IGF-1 LR3 have focused on IGF-1 receptor activation models and downstream intracellular signaling pathways. Research frameworks evaluate receptor-mediated interaction, kinase activation cascades, and cellular regulatory mechanisms under controlled in vitro and preclinical conditions.

1 of the 4 areas below are addressed directly by a paper cited on this page.

IGF-1 receptor activation models

No paper cited on this page reports on receptor or activation. This heading marks where IGF-1 LR3 is discussed in the category rather than a question the cited literature answers, and it is worth knowing which of these areas has work behind it and which does not.

Intracellular signaling pathway research

No paper cited on this page reports on intracellular. This heading marks where IGF-1 LR3 is discussed in the category rather than a question the cited literature answers, and it is worth knowing which of these areas has work behind it and which does not.

Growth-related regulatory framework studies

Addressed on this page by Hintz 1988. Each is linked to its source record in the references below, so what was measured — and in what system — can be read rather than taken on trust.

  • Hintz, R. et al. (1988) A sensitive radioimmunoassay for somatomedin-C/insulin-like growth-factor I based on synthetic insulin-like growth factor 57-70.

Receptor-binding dynamic investigations

No paper cited on this page reports on receptor, binding or dynamic. This heading marks where IGF-1 LR3 is discussed in the category rather than a question the cited literature answers, and it is worth knowing which of these areas has work behind it and which does not.

The references section of this page cites 3 primary papers published between 1988 and 2021 — a thin record. Every citation is linked to its PubMed or DOI record so it can be read rather than taken on trust, and the summaries above describe what those papers report rather than what the compound is claimed to do.

Research compounds attract claims that outrun their evidence. Below are the ones most often encountered for IGF-1 LR3, set against what the papers cited on this page actually report. Where the record is thin or contested, that is stated rather than smoothed over.

Also called

IGF-1 LR3 is also referred to as long R3, IGF.

Preclinical only

Described online as a muscle-building compound, on the basis of a longer active window than native IGF-1.

IGF-1 LR3 is a modified insulin-like growth factor engineered for reduced binding-protein affinity, which is the basis of the extended-activity description. The published work on it is laboratory research on receptor binding and cell proliferation. Growth factors that promote cell proliferation warrant particular caution, and no human clinical safety or efficacy data has been published for this analogue.

Nothing above is a statement of what this material does. It is a summary of what has been published and what has not. Eppix Labs supplies research materials only and provides no dosing, administration or protocol guidance.

Verification for IGF-1 LR3 is per lot, not per product. The current 1mg lot IGF1-CA-26A-01 returned 98.587% purity, 1.12 mg measured, 112% of the labelled 1 mg, assayed by Janoshik. Those figures are the laboratory's, published in full rather than reduced to a badge.

Purity is half the number. It states what fraction of the material in the vial is IGF-1 LR3; it says nothing about how much material is in the vial, and a short-filled vial can return a purity result that is entirely accurate. The figure that answers the second question is measured mass against expected content — for IGF-1 LR3, this lot measured 112% of its labelled 1 mg. Both numbers are published for every lot, whichever way they fall.

The lot code printed on the vial matches the code on the certificate for IGF-1 LR3. Matching the two is what confirms the unit in hand came from the batch that was tested — a certificate not tied to a lot code proves nothing about any particular unit.

Researchers who buy IGF-1 LR3 in the United States through Eppix Labs receive the lot described by the certificate above: the code printed on the vial label is the code on the certificate, and both are searchable on the batch verification page.

Verify a batch code →

Lyophilized storage
−20 °C long-term; stable at room temperature in transit
After reconstitution
2–8 °C
Light
Protect from UV and direct light
Freeze-thaw
Avoid repeated cycles
Vehicle
Bacteriostatic water in most published protocols
Format
Lyophilized powder

IGF-1 LR3 is supplied as lyophilized powder. In the dry state the material is comparatively stable, which is why it ships at ambient temperature without a cold chain; once reconstituted it is a peptide in solution and the handling constraints tighten considerably. At 14 residues it is short enough to be produced by solid-phase synthesis, and the published sequence on this page is what an identity assay is checked against.

Repeated freeze-thaw cycling is the handling error most likely to degrade material of this class, because each cycle concentrates solutes at the ice boundary. Where a protocol calls for the same vial across multiple sessions, the published literature generally describes aliquoting after reconstitution rather than re-freezing the whole volume.

Vials may appear empty on arrival. Lyophilized material collects at the base of the vial and is often not visible until the vial is inspected under direct light.

Reconstitution calculator →

Included
  • 1 × sealed glass vial in the strength selected (1mg / Single Vial, 1mg / 5-Pack, 1mg / 10-Pack available), batch-labelled
  • The batch-linked Certificate of Analysis for the exact lot shipped
  • Discreet outer packaging with no product names on the exterior
  • FedEx, tracked, typically 1–3 business days domestically
Not included
  • Bacteriostatic water or any other reconstitution vehicle
  • Syringes, needles or filters
  • Dosing, administration or protocol guidance of any kind

Reconstitution materials are sourced separately. The reconstitution calculator on this site works out concentrations for a given volume, but it is an arithmetic tool for laboratory record-keeping and not a protocol.

No. Eppix Labs products are supplied exclusively for laboratory research. We do not provide dosing, administration, or usage guidance.

Each vial contains 1mg of lyophilized IGF-1 LR3. Independent third-party testing verifies purity, identity, and net content per batch.

The vial contains only the peptide preparation. Any laboratory materials required for experimental procedures must be sourced separately.

Duration depends entirely on research protocol, storage conditions, and laboratory application.

Xia, J. et al.(2021)

MicroRNA‑29‑3p regulates the β‑catenin pathway by targeting IGF1 to inhibit the proliferation of prolactinoma cells. Mol Med Rep 23(6):437.

PubMed
Santucci, D. et al.(1994)

IGF-I and IGF-I24-41 but not IGF-I57-70 affect somatic and neurobehavioral development of newborn male mice. Brain Res Bull 36(1):27–32.

PubMed
Hintz, R. et al.(1988)

A sensitive radioimmunoassay for somatomedin-C/insulin-like growth-factor I based on synthetic insulin-like growth factor 57-70.

PubMed

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