Independent · non-commercial · publishes on a quarterly cycle|Current cycle 2026 Q3
Compound Evidence InstituteEvidence synthesis · established 2023Graded assessments of compounds, trials, methods and supply
Document set current to 30 July 2026
Compound monograph · §6–7

IGF-1 LR3 — analytical characterisation

Chromatographic conditions, identity, related substances, presentation, reconstitution and in-use stability.

Document identifier
CEI-MN-029/6
Series
Compound monograph
Version
3.0
Published
18 Feb 2024
Last reviewed
18 Jun 2024
Next review
18 Jun 2026
Identifier
10.71829/cei.mono.29
Certainty
Very low
Cycle
2024 Q1

§6Analytical characterisation

§6.1Chromatographic conditions

Column
Size-exclusion chromatography for aggregates and correct folding; reverse-phase C4 or C8 wide-pore for intact analysis; peptide mapping for sequence confirmation
Mobile phase and gradient
Method-dependent
Detection
UV 280 nm
Retention
Not applicable in the small-peptide sense
Representative chromatographic traceIllustrative ultraviolet chromatogram at 214 nanometres showing the main peak and related substances.051015202530Retention time (minutes)Absorbance, 214 nm99.70 % area
Figure 7. Illustrative. Representative ultraviolet trace at 214 nanometres constructed by the Institute to show the relationship between a main peak, its related substances and the reported area percentage. The trace is generated from a seeded model and is not a chromatogram of any material. It is published to make the integration question concrete: the same material analysed on a shallower gradient would resolve peaks that this trace co-elutes, and would report a lower purity.

§6.2Identity by mass spectrometry

Intact mass by high-resolution MS should return approximately 9111 Da. Three disulfide bonds must be verified as correctly paired, which requires peptide mapping under non-reducing conditions — an analysis no research-supply certificate assessed by the Institute has included.[3]

§6.3Related substances and degradation

Table 7. Related substances recorded for IGF-1 LR3, with the process or storage route that generates each and its analytical signature.

Related substanceOriginAnalytical signature
Misfolded and scrambled-disulfide speciesRefolding failure after bacterial expressionThe dominant quality risk for any recombinant protein with three disulfides; biologically inactive or aberrantly active, and invisible to reverse-phase purity
AggregatesRefolding and storageSize-exclusion chromatography
Host-cell protein and endotoxinBacterial expressionImmunoassay and the bacterial endotoxin test. Endotoxin is a specific concern for any bacterially expressed protein and is rarely reported
Truncated and clipped speciesProteolysis during productionReduced electrophoresis or peptide mapping
Residual methionine at the N-terminusIncomplete processing+131 Da
Degradation routes
  • Aggregation
  • Disulfide scrambling
  • Deamidation
  • Oxidation

§7Presentation, reconstitution and storage

§7.1Presentation and reconstitution

Presentation
Lyophilised powder in vial (research supply only)
Reconstitution
Research vials are commonly 1 mg. A 1 mg vial with 1.0 mL gives 1 mg/mL, at which 50 µg is 0.05 mL, that is 5 units on a U-100 syringe.
Storage, lyophilised
−20 °C or below, desiccated
Storage, reconstituted
2–8 °C for short periods; recombinant proteins in dilute solution without a carrier protein adsorb to container surfaces and lose content measurably
In-use period
No supported claim

The Institute includes this monograph principally to record a boundary: a bacterially expressed, three-disulfide recombinant protein cannot be assessed by a peptide purity certificate, and the assays that would matter — correct disulfide pairing, aggregate content, endotoxin — are not being performed anywhere in this supply channel.

§7.2In-use stability

Applicable standards: CEI-MS-01 · CEI-MS-02 · CEI-MS-03 · CEI-MS-04 · CEI-MS-05 · CEI-MS-06. The full series is at methodological standards.

Working calculators: reconstitution and insulin-unit conversion · purity against peptide content · certificate minimum-data checker.

References cited on this page

References are numbered in order of first citation in this document. Each superscript in the text links to its entry below.

  1. United States Pharmacopeial Convention. General Chapter ⟨1225⟩ Validation of Compendial Procedures. United States Pharmacopeia — National Formulary (USP–NF) 2024;USP 2024 Issue 1. identifier not held by the Institute
  2. International Council for Harmonisation of Technical Requirements for Pharmaceuticals for Human Use. ICH Q2(R2) Validation of Analytical Procedures. ICH Harmonised Guideline 2023;Step 4 version, 1 November 2023. identifier not held by the Institute
  3. International Council for Harmonisation of Technical Requirements for Pharmaceuticals for Human Use. ICH Q6B Specifications: Test Procedures and Acceptance Criteria for Biotechnological/Biological Products. ICH Harmonised Tripartite Guideline 1999;Step 4 version. identifier not held by the Institute
  4. International Council for Harmonisation of Technical Requirements for Pharmaceuticals for Human Use. ICH Q1A(R2) Stability Testing of New Drug Substances and Products. ICH Harmonised Tripartite Guideline 2003;Step 4 version. identifier not held by the Institute
  5. Manning MC, Chou DK, Murphy BM, Payne RW, Katayama DS. Stability of protein pharmaceuticals: an update. Pharmaceutical Research 2010;27(4):544–575. doi:10.1007/s11095-009-0045-6 · PMID 20143256

Identifiers are reproduced only where the Institute holds them. Where a digital object identifier or PubMed identifier is not shown, the Institute has recorded the journal and year and has not constructed an identifier.

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