Recombinant Human LR3 IGF-I/IGF-1 Protein, CF

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Recombinant Human LR3 IGF-I/IGF-1 Protein, CF Data
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Recombinant Human LR3 IGF-I/IGF-1 Protein, CF Summary

A synthetic analog of IGF-1 designed specifically to excel in cell culture applications

Features and Benefits
  • High Purity Is determined by SDS-PAGE (>95%) and reverse phase HPLC (>90%). This is the purest commercially available recombinant human LR3 IGF-1 (Figure 1). The high purity generates excellent performance of the protein.
  • Stability Extended half-life in culture provides cost saving and time saving benefits.
  • Low Endotoxin R&D Systems' endotoxin specification of <0.01 EU/ug of protein greatly diminishes potential non-specific effects in culture applications.
  • Lot-to-Lot Consistency Our robust manufacturing process includes stringent testing and analysis to ensure the same performance across all lots.
  • Multigram quantities are available to meet bioproduction demands.
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Measured in a serum-free cell proliferation assay using MCF‑7 human breast cancer cells. Karey, K.P. et al. (1988) Cancer Research 48:4083. The ED50 for this effect is 0.3-1.5 ng/mL. IGFBP-3 does not inhibt its activity.
E. coli-derived human IGF-I/IGF-1 protein
(Gly49-Ala118 (Glu51Arg))
Accession # P05019
N-terminus C-terminus 
Accession #
N-terminal Sequence
Predicted Molecular Mass
9 kDa
7 kDa, reducing conditions

Product Datasheets

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


Formulation Lyophilized from a 0.2 μm filtered solution in phosphate buffer, pH 7.2.
Reconstitution Reconstitute at 500 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Data Images

Bioactivity View Larger

Recombinant Human LR3 IGF-I/IGF-1 (Catalog # 8335-G1) stimulates cell proliferation in a serum-free assay using the MCF-7 human breast cancer cell line. The ED50for this effect is 0.3-1.5 ng/mL.

SDS-PAGE View Larger

1 μg/lane of Recombinant Human LR3 IGF-I/IGF-1 was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 7 kDa.

Mass Spectrometry View Larger

ESI analysis of Recombinant Human LR3 IGF-I/IGF-1 (Catalog # 8335-G1). The peak at 9112 Da corresponds to the calculated molecular mass, 9118 Da.

Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.


Background: IGF-I/IGF-1

Insulin-like Growth Factor I (IGF-I), also known as Somatomedin C, is the dominant effector of Growth Hormone (GH) and is structurally homologous to Proinsulin. Human IGF-I is synthesized as two precursor isoforms with N- and alternative C‑terminal propeptides (1). These isoforms are differentially expressed by various tissues (1). The 7.6 kDa mature IGF‑I is identical between isoforms and is generated by proteolytic removal of the N- and C-terminal regions. Mature human IGF-I shares 94% and 96% amino acid (aa) sequence identity with the mouse and rat orthologs, respectively (2). GH stimulates the production of IGF-I in most tissues (3). Hepatocytes produce circulating IGF-I, while local IGF-I is produced by many other tissues in which it has paracrine effects (1). IGF-I induces the proliferation, migration, and differentiation of a wide variety of cell types during development and postnatally (4, 5). IGF-I regulates glucose, fatty acid, and protein metabolism, steroid hormone activity, and cartilage and bone metabolism (6-11). It plays an important role in muscle regeneration and tumor progression (1, 12, 13). IGF-I binds IGF-I R, IGF-II R, and the Insulin Receptor, although its effects are mediated primarily by IGF-I R (14). IGF-I also binds with strong affinity to IGF binding proteins (IGFBPs), which regulate the availability and biological activities of IGF-I (15, 16).

Long R3 IGF-I (LR3 IGF-I) is a 9.2 kDa synthetic analog of IGF-I that is generated by modifying the aa sequence for mature human IGF-I. These modifications include the substitution of an Arg for Glu at position 3 of the mature IGF-1 sequence and the addition of a thirteen aa N-terminal extension, which is derived from methionyl porcine Growth Hormone (17). These aa changes generate a protein that is still capable of binding to IGF-I and Insulin receptors, but shows considerably lower affinity binding to IGFBPs compared to wild-type IGF-I (17, 18). As a result, LR3 IGF-I has an increased half-life and displays increased biological potency compared to IGF-I (17-22).

  1. Philippou, A. et al. (2007) In Vivo 21:45.
  2. Sandberg-Nordqvist, A.C. et al. (1992) Brain Res. Mol. Brain Res. 12:275.
  3. Berryman, D.E. et al. (2013) Nat. Rev. Endocrinol. 9:346.
  4. Guvakova, M.A. (2007) Int. J. Biochem. Cell Biol. 39:890.
  5. Sadagurski, M. and M.F. White (2013) Endocrinol. Metab. Clin. North Am. 42:127.
  6. Clemmons, D.R. (2006) Curr. Opin. Pharmacol. 6:620.
  7. Bluher, S. et al. (2005) Best Pract. Res. Clin. Endocrinol. Metab. 19:577.
  8. Garcia-Segura, L.M. et al. (2006) Neuroendocrinology 84:275.
  9. Malemud, C.J. (2007) Clin. Chim. Acta 375:10.
  10. Ling, P.R. et al. (1995) Am. J. Clin. Nutr. 61:116.
  11. Sheng, M.H. et al. (2014) J. Bone Metab. 21:41.
  12. Samani, A.A. et al. (2007) Endocrine Rev. 28:20.
  13. Gallagher, E.J. et al. (2010) Endocr. Pract. 16:864.
  14. LeRoith, D. and S. Yakar (2007) Nat. Clin. Pract. Endocrinol. Metab. 3:302.
  15. Denley, A. et al. (2005) Cytokine Growth Factor Rev. 16:421.
  16. Duan, C. and Q. Xu (2005) Gen. Comp. Endocrinol. 142:44.
  17. Francis, G.L. et al. (1992) J. Mol. Endocrinol. 8:213.
  18. Voorhamme, D. and C.A. Yandell (2006) Mol. Biotechnol. 34:201.
  19. Tomas, F.M. et al. (1993) Biochem. J. 291:781.
  20. Tomas, F.M. et al. (1996) J. Endocrinol. 150:77.
  21. Tomas, F.M. et al. (1997) J. Endocrinol. 155:377.
  22. von der Thüsen, J.H. et al. (2011) Am. J. Pathol. 178:924.
Long Name
Insulin-like Growth Factor I/Insulin-like Growth Factor 1
Entrez Gene IDs
3479 (Human); 16000 (Mouse); 24482 (Rat)
Alternate Names
IBP1; IGF1; IGF-1; IGF1A; IGFI; IGF-I; IGF-IA; IGF-IB; insulin-like growth factor 1 (somatomedin C); insulin-like growth factor 1; insulin-like growth factor I; insulin-like growth factor IA; insulin-like growth factor IB; Mechano growth factor; MGF; Somatomedin A; Somatomedin C; somatomedin-C


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