|Purity||>98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant hIGF-I. All lots are greater than 98% pure.|
|Endotoxin||Less than 0.01 ng endotoxin/1 μg hIGF-I.|
|Activity||The bioactivity of recombinant hIGF-I was determined in a cell proliferation assay using primary human dermal fibroblasts. The ED50 of each lot is between 2-8 ng/ml.|
|Molecular Formula||Recombinant hIGF-I has a Met on the amino terminus and has a calculated MW of 7,785. DTT-reduced and non-reduced protein migrate as 6 kDa polypeptides. The expected amino-terminal MGPET of recombinant hIGF-I was verified by amino acid sequencing.|
Recombinant human IGF-I (hIGF-I) Gly49-Ala118 (Accession #P01343) was produced in E. coli at Cell Signaling Technology.
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 IGF-I binding to 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).
UniProt ID: P05019
Entrez-Gene Id: 3479
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|8917SC||50 µg (With Carrier)||
|8917SF||50 µg (Carrier Free)||