| 货号 | 9897SC |
| 供应商 | CST |
| 背景 | Most circulating endocrine-acting IGF-I is produced by hepatocytes, and paracrine- or autocrine-acting IGF-I is produced by defined cell types within specific tissues (1,2). Many neoplastic cells produce IGF-I, which regulates a number of cellular processes including energy metabolism, proliferation, and cell survival (3,4). IGF-I activity is regulated by one or more of the six extracellular IGF-binding proteins (IGFBPs). IGFBPs bind to IGF-I, and most inhibit the binding between IGF-I and the IGF-I receptor (IGFIR) (1,2). Some IGFBPs may increase cell responses to IGF-I. Binding of IGF-I to IGFIR activates the Akt, JNK, and Erk pathways (2). IGF-I and IGFIR are frequently expressed by cancer cells and may contribute to the proliferation and viability of a number of cancer types (1,2). |
| 存放说明 | 4C |
The purity of recombinant mIGF-I was determined by SDS-PAGE of 6 µg reduced (+) and non-reduced (-) recombinant mIGF-I and staining overnight with Coomassie Blue. | |
The proliferation of primary human dermal fibroblasts treated with increasing concentrations of mIGF-I was assessed. After 72 hour treatment with mIGF-I, cells were incubated with a tetrazolium salt and the OD450 - OD650 was determined. | |
Western blot analysis of extracts from NIH/3T3 cells, untreated or treated with increasing concentrations of mIGF-I for 10 minutes, using Phospho-Akt (Ser473) (D9E) XP® Rabbit mAb #4060 (upper) and Akt1 (C73H10) Rabbit mAb #2938 (lower). | |
The ability of mIGF-I to induce phosphorylation of Akt was assessed. After serum starvation, NIH/3T3 cells were treated with increasing concentrations of mIGF-I for 10 minutes. Cells were lysed, and phospho-Akt was quantified using PathScan® Phospho-Akt (Thr308) Sandwich ELISA Kit #7252. OD450 is shown. |
