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I8904 Sigma

Insulin-like Growth Factor-II from mouse

IGF-II, recombinant, expressed in E. coli, lyophilized powder

Synonym: IGF-II

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Description

Analysis Note

The biological activity is measured in a serum-free cell proliferation assay using the human breast carcinoma cell line MCF-7.

Packaging

50 μg in poly bottle

Physical form

Lyophilized from a 0.2 μm filtered solution of 30% acetonitrile and 0.1% of TFA.

Biochem/physiol Actions

Insulin-like growth factor II (IGF-II) is a potent mitogenic growth factor that mediates growth-promoting activities in embryonic development. IGF-II binds the IGF-II receptor with high affinity. IGF-I and IGF II are expressed in many tissues and cell types. IGF-II is mitogenic for a variety of cultured cells including human or chicken fibroblasts, mouse 3T3 cells, normal rat kidney.

General description

Recombinant Mouse IGF-II is produced from a DNA sequence encoding the mature IGF-II protein. Mouse IGF-II, a 67 amino acid protein, has a predicted molecular matrix of ~7.4 kDa. Mouse and human IGF-II share 91% sequence homology. Insulin-like growth factor II (also known as multiplication stimulating activity or MSA) and insulin-like growth factor I (IGF-I) belong to the family of insulin-like growth factors, which are structurally homologous to proinsulin. Mature IGF-I and IGF-II are highly conserved and share ~70% amino acid sequence identity. They have autocrine, paracrine, and endocrine functions.

Price and Availability


All labs need water
Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
3

Documents

Certificate of Analysis

Certificate of Origin

Protocols & Articles

Articles

Insulin-like Growth Factors (IGF)

Insulin-like growth factors (IGF-I and IGF-II) are mitogenic and anabolic peptides structurally homologous to insulin. IGF-I and -II are single polypeptide chains of approximately 7.5 kDa comprised o...
Jennifer Fries
BioFiles 2009, 4.5, 12.
Keywords: Adhesion, Apoptosis, Biofiles, Cancer, Growth factors, Hormones, Infrared spectroscopy, Ligands, Transduction, transformation

Peer-Reviewed Papers
15

References

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