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Description:
Human Insulin-like Growth Factor-II (Human IGF-II) is synthesized as a 156 amino acid precursor protein, known as proIGF-II. This protein includes an 87 amino acid C-terminal region known as the E-domain. A proteolysis step releases the mature 67 amino acid IGF-II polypeptide. The proIGF-II proteins make up 10-20% of circulating IGF-II. Pro-IGF-II proteins are secreted by some tumor cell lines and levels are elevated in non-islet cell tumor hypoglycemia.
References:
Duguay S. J. et al. (1998) J . Biol. Chem. 273, 18443-18451.
Source:
Produced recombinantly in E.coli.
Purity:
> 85 % (determined by HPLC and N-terminal sequence analysis).
Molecular Weight:
The final product contains three major isoforms of proIGF-II corresponding to molecular weights of 16.1, 17.0 and 17.6 kDa.
These species correspond to the full length 156 amino acid protein and two smaller species corresponding to C-terminal truncations of approximately 5 and 15 residues which result from the purification process.
N-terminal sequence analysis:
5 residues > 85 % single sequence
Biological Activity:
Stimulation of protein synthesis in rat L6 myoblasts.
Endotoxin:
< 0.1 EU/µg
State and Appearance:
Lyophilized white powder.
Dried from 0.1 M acetic acid and stored under dry nitrogen at a slight vacuum (-25 kPa)
Storage/Stability:
At least 2 years at 2 - 4°C (lyophilized).
Detection:
By Western blot
Reconstitution:
#1000: Handling of Novozymes GroPep IGF-I, IGF-II and IGF Analogs
Protocol:
#3009: Procedure for Western Immunoblotting human ProIGF-II
Related Products:
Human proIGF-II (aa 1-104)
IGF-IIE, (aa 138 - 156), anti-human
IGF-IIE, (aa 89 - 101), anti-human
IGF-IIE, (aa 78 - 88), anti-human
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