Serial dilutions of Mouse IGF-I Recombinant Protein were added to FDC-P1 cells. Cell proliferation was measured and the linear portion of the curve was used to calculate the ED50.
The purity of Mouse IGF-I Recombinant Protein was determined by SDS-PAGE of 1 µg reduced (+) and non-reduced (-) recombinant mIGF-I and staining with Coomassie Blue.
Mouse IGF-I Recombinant Protein is supplied as lyophilized material that is very stable at -20°C. It is recommended to reconstitute with sterile water at a concentration of 0.1 mg/ml which can be further diluted in aqueous solutions as needed. Addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage.
A greater than or equal to 95% purity was determined by SDS-PAGE.
Endotoxin levels are less than or equal to 1 EU / 1 μg mIGF-I.
The bioactivity of recombinant mIGF-I was determined in an FDC-P1 cell proliferation assay. The ED50 of each lot is less than or equal to 20 ng/ml.
Recombinant mouse IGF-I was expressed in E. coli and is supplied in a lyophilized form.
Most circulating endocrine-acting insulin-like growth factor I (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 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).
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