Product Pathways - Growth Factors/Cytokines
Human Insulin-like Growth Factor II (hIGF-II) #5238
|5238SF||50 µg (Carrier Free)||---||In Stock||---|
|5238SC||50 µg (With Carrier)||---||In Stock||---|
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Recombinant human IGF-II (hIGF-II) Ala25-Glu94 (Accession # P01344-2) was produced in E. coli at Cell Signaling Technology.
Recombinant hIGF-II does not have a Met on the amino terminus and has a calculated MW of 7,606. DTT-reduced and non-reduced protein migrate as 6 kDa polypeptides. The expected amino-terminal AYRPS of recombinant hIGF-II was verified by amino acid sequencing.
>98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant hIGF-II. All lots are greater than 98% pure.
The bioactivity of recombinant hIGF-II was determined in a cell proliferation assay using primary human dermal fibroblasts. The ED50 of each lot is between 10-20 ng/ml.
The purity of recombinant hIGF-II was determined by SDS-PAGE of 6 µg reduced (+) and non-reduced (-) recombinant hIGF-II and staining overnight with Coomassie Blue.
The proliferation of primary human dermal fibroblasts treated with increasing concentrations of hIGF-II was assessed. After 72-hour treatment with hIGF-II, cells were incubated with a tetrazolium salt and the OD450 - OD650 was determined.
Western blot analysis of extracts from human dermal fibroblasts untreated or treated with hIGF-II for 10 minutes, using Phospho-Akt (Ser473) (D9E) XP® Rabbit mAb #4060 (upper) and Akt1 (C73H10) Rabbit mAb #2938 (lower).
Less than 0.01 ng endotoxin/1 μg hIGF-II.
With carrier: Lyophilized from a 0.22 μm filtered solution of 20 mM citrate, pH 3.0 containing 100 mM NaCl and 20 μg BSA per 1 μg hIGF-II. Carrier free: Lyophilized from a 0.22 μm filtered solution of 20 mM citrate, pH 3.0 containing 100 mM NaCl.
IGF-II is a potent cellular mitogen that is closely related to IGF-I (1). IGF-II is primarily produced by the liver and is frequently overexpressed in tumors (1,2). IGF-II binds to the IGF-IR, activating the AKT, mTOR, ERK, and JNK pathways (1). IGF-II signaling is regulated by several distinct mechanisms. First, IGF binding proteins (IGFBPs) bind to IGF-II and block interactions with the IGF-IR (1-3). Second, the IGF-IIR, binds to and acts as a molecular trap for IGF-II (1-3). Lastly, the IGF2 gene is an imprinted gene, and loss of imprinting leads to increased IGF-II levels (1-3). Aberrant levels of IGF-II are associated with Wilms tumor, Beckwith-Wiedmann syndrome, and colorectal cancer (1,2).
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