purified, E. coli-derived recombinant human insulin-like growth factor-I.
Biochem/physiol Actions
Insulin-like growth factor -1 shares structural homology with proinsulin and is mainly produced by liver. IGF-1 acts via specific receptor, IGF-1R, a heterodimeric tyrosine kinase receptor that signals to various second messenger pathways such as MAPK, Raf/Ras and PI3K cascades. The effects of IGF-1R signaling are important at many developmental levels from cells to organ to organism, growth, differentiation, anti-apoptosis, proliferation and transformation.
Physical form
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline with 5% trehalose.
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The insulin receptor (IR) and the insulin-like growth factor I receptor (IGF-IR) belong to the same subfamily of receptor tyrosine kinases with two extracellular alpha-subunits and two transmembrane beta-subunits. They share a high similarity of structure and intracellular signalling events.
The last decade has been characterized by a major investigative thrust into the physiology of two unique but ubiquitous peptides, insulin-like growth factor (IGF)-I and IGF-II. The regulatory systems that control the tissue bioactivity of the IGFs have been delineated
The American journal of pathology, 178(1), 26-31 (2011-01-13)
Insulin and insulin-like growth factors (IGFs) are important regulators of energy metabolism and growth. Several findings have outlined an important role played by this family of molecules in both tumor maintenance and development. Despite the established contribution of the IGF
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