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Description:
The IGF-II gene encodes a single transcript which results in an 156 amino acid protein, including an 89 amino acid E-domain. ProIGF-II contains sites of O-linked glycosylation. ProIGF-II is converted to mature IGF-II by sequential cleavage after amino acids 104, 87 and 67. Differential glycosylation and cleavage within the E-domain can therefore result in multiple proIGF-II isoforms.
The proIGF-II proteins make up 10-20% of circulating IGF-II. ProIGF-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:
> 95% by HPLC and N-terminal sequence
Molecular Weight:
11949 Da
N-terminal sequence analysis:
5 residues > 95% single sequence
Biological Activity:
Stimulation of protein synthesis in rat L6 myoblasts.
Endotoxin:
< 0.1 EU/ug
State and Appearance:
Lyophilized white powder.
Dried from 0.1M acetic acid under dry nitrogen at a slight vacuum
(-25 kPa)
Storage/Stability:
At least 2 years at 2 - 4oC (lyophillized).
Detection:
By Western blot
Reconstitution:
#1000: Handling of GroPep Bioreagents IGF-I, IGF-II and IGF Analogs
Protocol:
#3009: Procedure for Western Immunoblotting human ProIGF-II
Related Products:
Human proIGF-II (aa 1-156)
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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