IGF-I fusion polypeptides and therapeutic uses thereof

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Hormones – e.g. – prolactin – thymosin – growth factors – etc.

Reexamination Certificate

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Details

C530S350000, C530S387300, C536S023400

Reexamination Certificate

active

07396918

ABSTRACT:
A fusion protein comprising at least one IGF1 variant component and a fusion component (F), and, optionally, a signal sequence, exhibiting improved stability relative to the native IGF1 or IGF2 polypeptide. The fusion component (F) may be a multimerizing component, a targeting ligand, or another active or therapeutic compound. IGF1 variants were shown to have improved ability to induce skeletal muscle hypertrophy relative to native IGF1.

REFERENCES:
patent: 0742228 (1996-11-01), None
patent: WO 09/15142 (1990-12-01), None
Bayne et al., The C region of human insulin-like growth factor (IGF) I is required for high affinity binding to the type 1 IGF receptor, 1998, The Journal of Biological Chemistry, vol. 254, Issue 19, pp. 11004-11008.
Jansson et al., The insulin-like growth factor (IGF) binding protein 1 binding epitope on IGF-I probed by heteronuclear NMR spectroscopy and mutational analysis, 1998, vol. 273, Issue 38, The Journal of Biological Chemistry, vol. 273, Issue 38, pp. 24701-24707.
Heding et al., Biosensor measurement of the binding of insulin-like growth factors I and II and their analogues to the insulin-like growth factor-binding protein-3, 1996, The Journal of Biological Chemistry, vol. 271, Issue 24, pp. 13948-13952.
Jansson, M., S.A., et al., (1997) Biochemistry 36:4108-4117.

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