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Recombinant Human IGF-I Protein, 100µg  

Recombinant Human IGF-I Protein, 100µg

Recombinant Human IGF-I Protein, With N-Fc Tag (rhIGFI-Fc) Gly 49 - Ala 118 was produced in human 293 cells (HEK293)

Synonyms: IGF-I, IGF1A, somatomedin C, MGF, Insulin-like growth factor 1 (IGF-1),sulfation factor, IGF-1 protein

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216,00 €

Background: Insulin-like growth factor 1 (IGF-1) also known as somatomedin C, IGF1A, IGFI, sulfation factor, and is a hormone similar in molecular structure to insulin. It plays an important role in childhood growth and continues to have anabolic effects in adults. A synthetic analog of IGF-1, mecasermin is used for the treatment of growth failure. IGF-1 consists of 70 amino acids in a single chain with three intramolecular disulfide bridges. IGF-1 has a molecular weight of 7649 daltons. IGF-1 is produced primarily by the liver as an endocrine hormone as well as in target tissues in a paracrine/autocrine fashion. IGF-1 binds to at least two cell surface receptors: the Insulin-like growth factor 1 receptor, abbreviated as "IGF1R", and the insulin receptor. The IGF-1 receptor seems to be the "physiologic" receptor - it binds IGF-1 at significantly higher affinity than the IGF-1 that is bound to the insulin receptor. Like the insulin receptor, the IGF-1 receptor is a receptor tyrosine kinase - meaning it signals by causing the addition of a phosphate molecule on particular tyrosines. Its primary action is mediated by binding to its specific receptor IGF1R, present on many cell types in many tissues. Binding to the IGF1R, a receptor tyrosine kinase, initiates intracellular signaling; IGF-1 is one of the most potent natural activators of the AKT signaling pathway, a stimulator of cell growth and proliferation, and a potent inhibitor of programmed cell death. Insulin-like growth factor 1 has been shown to bind and interact with all the IGF-1 Binding Proteins (IGFBPs), of which there are six (IGFBP1-6). Specific references are provided for interactions with IGFBP3, IGFBP4 and IGFBP7.

Recombinant Human IGF-I Protein, With N-Fc Tag (rhIGFI-Fc) Gly 49 - Ala 118 (Accession # P05019) was produced in human 293 cells (HEK293).

Molecular Characterization
This protein carries a human IgG1 Fc tag at the N-terminus.
The protein has a calculated MW of 35.0 kDa. The protein migrates as 40 kDa under reducing (R) condition (SDS-PAGE).

Less than 1.0 EU per μg of the rhIGFI-Fc by the LAL method.

>98% as determined by SDS-PAGE.

Lyophilized from 0.22 μm filtered solution in 50 mM tris, 100 mM glycine, pH7.0. Normally Mannitol or Trehalose are added as protectants before lyophilization.

See Certificate of Analysis for details of reconstitution instruction and specific concentration.

Avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C-8°C); After reconstitution under sterile conditions for 1 month (4°C-8°C) or 3 months (-20°C to -70°C).

Measured in a serum-free cell proliferation assay using MCF-7 human breast cancer cells. The ED50 for this effect is typically 0.5-2.5 ng/mL.


(1) SALMON WD Jr, et al., 1957, J Lab Clin Med 49 (6): 825–36.
(2) Keating GM, et al., 2008, BioDrugs 22 (3): 177–88.
(3) Horton JK, et al., 1989, Biochem. Pharmacol. 38 (11): 1727–36.
(4) Ueki I, et al., 2000, Proc. Natl. Acad. Sci. U.S.A. 97 (12): 6868–73.
(5) Buckway CK, et al., 2001, J. Clin. Endocrinol. Metab. 86 (10): 4943–50.
(6) Qin X, et al., 1998, J. Biol. Chem. 273 (36): 23509–16.
(7) Ahmed S, et al, 2003, Biochem. Biophys. Res. Commun. 310 (2): 612–8.