IGF-1 (Pen)

Description

IGF-1 research pen — Canada

Researched & reviewed by the SPO Quality Team · Last reviewed: 30 September 2026

This listing is IGF-1 in pen format (1mg fill) — the same research material as our IGF-1 vials, supplied in a pre-formatted research pen for laboratories that prefer logged, repeatable handling over loose vials. Insulin-like growth factor 1 is not a designer peptide but a human hormone: a 70-amino-acid single-chain protein, cross-linked by three disulfide bridges, whose sequence Rinderknecht and Humbel published in 1978 and whose shape echoes proinsulin^[2]. It is the messenger through which growth hormone acts on cartilage and bone — the “sulphation factor” of 1957^[1], later renamed somatomedin C and then IGF-1^[6]. Because IGF-1 is a real drug in one rare condition and a doping concern in sport, this page is longer than most: there is no separate research guide for IGF-1 on this site, so the compound’s identity, history, laboratory literature and limits are set out here. Laboratory research only; the pen is a handling format, not an instruction.

Identity at a glance

Batch documentation: a batch-specific COA for the IGF-1 pen has not been posted yet — see the COA library. Reports for the vial listings, where posted, are on those pages.

Where IGF-1 comes from

The idea came before the molecule. In 1957 Salmon and Daughaday showed that growth hormone did not act on cartilage directly but through a serum factor that stimulated sulfate uptake^[1]. Two decades of purification ended with the 1978 sequence: 70 residues, three disulfides, an unmistakable resemblance to proinsulin^[2]. The receptor followed in 1986, when Ullrich’s group cloned a 1,367-residue precursor that is processed into α and β subunits like the insulin receptor, with a tyrosine-kinase domain in the β chain^[3]. Human genetics then fixed the hormone’s role: a 1996 report described intrauterine growth retardation and postnatal growth failure in a patient with a deletion of the IGF1 gene^[4], and Laron syndrome — growth-hormone insensitivity with very low IGF-1 — became the natural experiment for what happens when the signal is absent^{[6, 11]}.

What has been studied in the laboratory

• Liver-specific knockout (mouse, 1999): deleting Igf1 in the liver caused a dramatic fall in circulating IGF-1 yet body weight, body length and femur length matched wild-type littermates — evidence that locally produced IGF-1, not the circulating pool, drives most somatic growth^[5].
• Receptor biology (review, 2026): beyond the plasma membrane, the IGF-1 receptor is internalised and continues to signal from intracellular compartments, including the nucleus — a topic of oncology interest because IGF-1R signalling supports cell survival and proliferation^[12].
• Exercise and muscle (review, 2026): resistance exercise raises muscle IGF-1 and the PI3K/Akt and MAPK/ERK pathways downstream of it, which the authors frame as a route to counter age-related loss of muscle mass^[13]. That is a statement about endogenous IGF-1 in exercising muscle, not about exogenous protein.
• Cancer epidemiology (meta-analysis, 2016): circulating IGF-1 and IGF-binding proteins were examined against ovarian-cancer risk across the published cohorts^[10] — one of many studies that make IGF-1 a two-sided molecule in the literature.
• Ageing (review, 2023): people with Laron syndrome have low IGF-1 for life and a distinctive pattern of ageing and disease risk, which the authors use to test ideas about IGF-1 and longevity^[11].

The clinical and anti-doping context

Recombinant human IGF-1, mecasermin, is a regulated prescription medicine for children with severe primary IGF-1 deficiency: a 2007 report followed 76 such children through years of treatment and recorded growth responses alongside frequent adverse events — hypoglycaemia in 49% of treated children, injection-site lipohypertrophy in 32% and tonsillar/adenoidal hypertrophy in 22%^[7]; a 2013 review sets out how that rare diagnosis is made and treated^[8]. None of that transfers to a research vial — the medicine is a characterised pharmaceutical given under specialist care for a defined indication. IGF-1 is also an anti-doping problem: a 2013 review describes it as an attractive performance-enhancing agent, notes that IGF-1 compounds and analogues have been sold on the internet and black market for years, and reports that no test for its misuse was yet in place^[9]. The material on this page is sold for laboratory research and for no other purpose.

What the evidence does not show

• No research-grade IGF-1 has been shown to do anything in a person. Every human result cited above concerns mecasermin in children with a diagnosed deficiency^{[7, 8]}; the reviews of exercise, ageing and cancer describe the body’s own IGF-1^{[13, 11, 10]}.
• The circulating pool is not the whole story. Mice without hepatic IGF-1 grew normally^[5]; what a protein in a vial would do after leaving it is not inferable from serum-level correlations.
• The literature records risks, not only effects. Hypoglycaemia, lipohypertrophy and tonsillar/adenoidal hypertrophy were documented in the treatment cohort^[7], and IGF-1 signalling is a survival pathway in tumour cells^[12].
• Identity is not guaranteed by a name. “IGF-1” products vary between the native protein and analogues such as LR3; without a mass-spectrometry result the vial’s contents are a label, not a fact.

Storage and handling

• Follow the label: keep the pen cool, dry and out of light, and do not subject it to repeated freeze–thaw.
• Log the batch number and dates of receipt and first use, as with any research material. No protocol or administration information is provided here.

Vial strength: IGF-1 1MG. Other pens are on the peptide pens page; the whole range is on our buy peptides online in Canada page. Canada Post from inside Canada (shipping policy).

Related reading: IGF-1 vs IGF-1 LR3: Native Hormone vs Long R3 Analogue

Frequently asked questions

What is the IGF-1 pen?

The same synthetic IGF-1 supplied in a pre-formatted research pen rather than a loose vial, for laboratories that want repeatable, logged handling. It is a research format only; no administration guidance of any kind is given.

Is there a batch report for the IGF-1 pen?

Not yet. No batch-specific report for the pen is posted in the COA library. The page will state the report when one exists.

Is the IGF-1 pen for human use?

No. The pen is supplied for laboratory research only and is not for human or animal use. No dosing, administration or protocol information is provided.

References

Retrieved from PubMed (NCBI) on 30 September 2026 and cross-checked against Europe PMC; protein identity from UniProt (P05019).

1. SALMON WD, DAUGHADAY WH (1957). A hormonally controlled serum factor which stimulates sulfate incorporation by cartilage in vitro. J Lab Clin Med. PMID 13429201
2. Rinderknecht E, Humbel RE (1978). The amino acid sequence of human insulin-like growth factor I and its structural homology with proinsulin. J Biol Chem. PMID 632300
3. Ullrich A, Gray A et al. (1986). Insulin-like growth factor I receptor primary structure: comparison with insulin receptor suggests structural determinants that define functional specificity. EMBO J. PMID 2877871
4. Woods KA, Camacho-Hübner C et al. (1996). Intrauterine growth retardation and postnatal growth failure associated with deletion of the insulin-like growth factor I gene. N Engl J Med. PMID 8857020
5. Yakar S, Liu JL et al. (1999). Normal growth and development in the absence of hepatic insulin-like growth factor I. Proc Natl Acad Sci U S A. PMID 10377413
6. Laron Z (2001). Insulin-like growth factor 1 (IGF-1): a growth hormone. Mol Pathol. PMID 11577173
7. Chernausek SD, Backeljauw PF et al. (2007). Long-term treatment with recombinant insulin-like growth factor (IGF)-I in children with severe IGF-I deficiency due to growth hormone insensitivity. J Clin Endocrinol Metab. PMID 17192294
8. Savage MO (2013). Phenotypes, investigation and treatment of primary IGF-1 deficiency. Endocr Dev. PMID 23392102
9. Guha N, Cowan DA et al. (2013). Insulin-like growth factor-I (IGF-I) misuse in athletes and potential methods for detection. Anal Bioanal Chem. PMID 23934394
10. Gianuzzi X, Palma-Ardiles G et al. (2016). Insulin growth factor (IGF) 1, IGF-binding proteins and ovarian cancer risk: A systematic review and meta-analysis. Maturitas. PMID 27823741
11. Werner H, Laron Z (2023). Insulin-like growth factors and aging: lessons from Laron syndrome. Front Endocrinol (Lausanne). PMID 37941907
12. Zhang T, Li L et al. (2026). Beyond the membrane: Internalization and compartmentalization of insulin‑like growth factor 1 receptor signaling in cancer pathogenesis and treatment (Review). Int J Oncol. PMID 41716020
13. Liu Z, Tong X et al. (2026). Restoring the balance: Resistance exercise-induced insulin-like growth factor-1 restores PI3K/Akt and MAPK/ERK cross-talk to ameliorate Alzheimer's disease. Ageing Res Rev. PMID 42413217

For laboratory research use only; not for human or animal consumption. This page identifies the protein, its documentation status and its published literature, and makes no claim of efficacy or safety for the material sold.