IGF-I receptor is a disulfide-linked heterotetrameric transmembrane protein consisting of two alpha and two beta subunits. Both the alpha and beta subunits are encoded within a single receptor precursor cDNA. The proreceptor polypeptide is proteolytically cleaved and disulfide-linked to yield the mature heterotetrameric receptor. The alpha subunit of IGF-I receptor is extracellular while the beta subunit has an extracellular domain, a transmembrane domain and a cytoplasmic tyrosine kinase domain. The IGF-I receptor is highly expressed in all cell types and tissues.

Images: (1) Lysates were prepared from NTERA-2 human embryonal carcinoma cells, SK-MEL-28 human malignant melanoma cells, and G-361 human malignant melanoma cells in non-reducing sample buffer. The lysates were resolved by SDS-PAGE and transferred to an Immobilon-P membrane. The blot was developed with 1 μg/mL monoclonal anti-human IGF-I R antibody and WesternGlo Chemiluminescent Detection Substrate. (2) IGF-I R (at a dilution of 25 µg/mL) staining of paraffin-embedded human skin tissue. Tissue stained with anti-mouse HRP-DAB (Brown) and counterstained with haematoxylin (blue).

Other Reagents to Consider:

Antibodies

IGF-I R Flow Cytometry

IGF-II

IGFBP-3

All Neurotrophin and Growth Factors

Cancer Antibodies

All Diabetes and Obesity Antibodies

Pain/Inflammation Antibodies

All Stem Cell Reagents

Neuron/Glial Markers

Proteins

Neurotrophin and Growth Factor Proteins

All Diabetes and Obesity Proteins