Product Name
Insulin-like Growth Factor-I human, IGF-I, recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture
biological source
human
recombinant
expressed in E. coli
assay
≥95% (HPLC)
form
lyophilized powder
potency
0.1-10 ng/mL ED50/EC50
quality
endotoxin tested
mol wt
~7.6 kDa
packaging
pkg of 50 and 100 μg
technique(s)
cell culture | mammalian: suitable
impurities
≤1.00 EU/μg
UniProt accession no.
storage temp.
−20°C
Quality Level
Gene Information
human ... IGF1(3479), Igf1(16000)
Analysis Note
The biological activiy is calculated by the dose-dependent proliferation of murine BALBC/3T3 cells. ED50 corresponds to a specific activity of at least 1 x 105 units/mg.
Application
Insulin-like Growth Factor-I human has been used:
- in modified Dulbecco minimal essential medium for in vitro culture of testicular cells
- in culture media, to study its effect on steroidogenesis during testicular development
- in culture media for in vitro assay of splenic pro-erythroid cell growth and differentiation
Biochem/physiol Actions
IGF-I also known as somatomedin C, is secreted from the liver into circulation in a process regulated by pituitary growth hormone (GH) and so it mediates the growth-promoting activity of GH. In the developing embryo IGF-I is expressed primarily by mesenchymal-derived cells. After birth IGF-I expression in most extrahepatic tissues declines and hepatic expression of IGF-I becomes GH-regulated. Expression of IGF-I outside the liver is regulated differently, depending on the specific tissues. For example, gonadotropins and sex steroids regulate IGF-I expression within the reproductive system, while parathyroid hormone and sex steroids regulate IGF-I expression in bone. IGF-I is produced in several human tumors. IGF-I is mitogenic for a variety of cells including fibroblasts, osteoblasts, smooth muscle cells, fetal brain cells, neuroglial cells, and erythroid progenitor cells. IGF-I exerts its actions exclusively through the IGF-I receptor (IGF-IR). IGF-I induces endothelial cell migration and is involved in the regulation of angiogenesis.
IGF-I, also known as somatomedin C, mediates the growth-promoting activity of GH (growth hormone). IGF-I induces endothelial cell migration and is involved in the regulation of angiogenesis. IGF-I exerts its actions through the IGF-I receptor.
Insulin-like growth factor I (IGF-I) plays a critical role in cellular energy metabolism and growth and development, especially prenatal growth.
General description
Insulin-like growth factor I (IGF-I) is localized on human chromosome 12q23.2.
Physical form
Lyophilized from 0.2 μm filtered solution in 50 mM acetic acid.
Preparation Note
Reconstitute in water
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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A comparison of the effects of equine luteinizing hormone (eLH), equine growth hormone (eGH) and human recombinant insulin-like growth factor (hrIGF-I) on steroid production in cultured equine Leydig cells during sexual maturation
Hess MF and Roser JF
Animal Reproduction Science, 89(1-4), 7-19 (2005)
An optimized system for studies of EPO-dependent murine pro-erythroblast development
Zhang D, et al.
Experimental Hematology, 29(11), 1278-1288 (2001)
Juan E Puche et al.
Journal of translational medicine, 10, 224-224 (2012-11-15)
Insulin-like growth factor I (IGF-I) is a polypeptide hormone produced mainly by the liver in response to the endocrine GH stimulus, but it is also secreted by multiple tissues for autocrine/paracrine purposes. IGF-I is partly responsible for systemic GH activities
M J E Walenkamp et al.
Endocrine development, 24, 128-137 (2013-02-09)
Molecular defects of the insulin-like growth factor 1 gene (IGF1) are rare in the human. Only three homozygous and two families with heterozygous mutations of the IGF1 gene have been described, resulting in a variable degree of intrauterine and postnatal
Shu-Lin Liu et al.
Molecular cell, 71(6), 1092-1104 (2018-09-04)
Activation of class I phosphatidylinositol 3-kinase (PI3K) leads to formation of phosphatidylinositol-3,4,5-trisphophate (PIP3) and phosphatidylinositol-3,4-bisphophate (PI34P2), which spatiotemporally coordinate and regulate a myriad of cellular processes. By simultaneous quantitative imaging of PIP3 and PI34P2 in live cells, we here show
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