This product has recently been released.
This product is freeze dried. All water molecules have been removed.
The activity of this product has been verified and approved by our professional team.
This lyophilized product is shipped at room temperature. Please see its certificate of analysis for further storage instructions.
This vial contains 100% net peptide content.
0.1 EU per 1 µg of the protein by the LAL method & lyophilized from a 0.2 µm filtered solution.
The ED50 as determined by a cell proliferation assay using FDC-P1 cells is less than 2.0 ng/ml, corresponding to a specific activity of >500,000 units/mg.
rat IGF-I is fully biologically active when compared to standards. The ED50 shown in literature was calculated in two different methods: 1. Stimulation of protein synthesis in rat L6 myoblasts ED50 was found to be less than 30 ng/ml. 2. Type 1 IGF receptor binding assay ED50 was found to be less than 10 ng/ml.
IGF-I is a pleiotropic factor involved in multiple processes, so its actions are different depending on its concentration, the cell type, and the developmental stage of the animal1. IGF-I promotes proliferation of neural cells by interacting with the IGF-IR which may activate the PI3K/Akt or the MAP kinase pathways1.
Evidence indicates that IGF-I promotes cell survival by inhibiting apoptosis both in vivo and in vitro. IGF-I is also involved in the regulation of the migration of certain cell types1.
Insulin-like growth factor-I (IGF-I) belongs to the insulin family which is divided in two groups of peptides: 1- insulin and IGFs and 2- relaxin and insulin-like hormones. The structure of mature IGF-I is composed of a single polypeptide chain of 70 amino acids with 57 amino acids being identical across different organisms1,2.
IGF-I is a pleiotropic factor responsible for the regulation of several cellular processes depending on its concentration, cell type and the developmental stage of the organism.
IGF-I binds to IGF-I receptor and triggers the auto phosphorylation of the receptor and the activation of the insulin receptor substrates1.
In the embryonic brain IGF-I expression is relatively high and drops sharply in the adult brain except in the hippocampus and the subventricular zone-olfactory bulb. In adults IGF-I is mainly synthesized in the liver though a process regulated by the growth hormone (GH). IGF-I can cross the blood-brain-barrier by binding to the IGF-I receptor present on endothelial cells and is later picked up by astrocytes to be transferred to neurons or directly by neurons1,2.
Studies show that IGF-I influences neural stem cell proliferation and differentiation into neurons and glia as well as neuronal maturation including synapse formation. IGF-I also promotes adult neurogenesis by regulating neural stem cell number and differentiation1.
rat IGF-I (#I-200) is a highly pure and biologically active recombinant protein expressed in and extracted from E. coli.