Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Details of Functionality | Measured by its binding ability in a functional ELISA. When Recombinant Mouse (rm) IGF-I R/IGF1R is present at 0.5 μg/mL, the concentration of rmIGF-I that produces 50% of the optimal binding response is found to be approximately 10-60 ng/mL. |
Source | Chinese Hamster Ovary cell line, CHO-derived mouse IGF-I R/IGF1R protein Met1-His936 with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | Glu31 & Asp742 |
Structure / Form | Covalently-linked heterotetramers (2 alpha and 2 beta subunits) & covalently-linked single chain homodimers |
Protein/Peptide Type | Recombinant Proteins |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 104.5 kDa (single chain), 80.7 kDa ( alpha subunit) & 23.2 kDa ( beta subunit). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 160-170 kDa, 120-130 kDa & 45-52 kDa, reducing conditions. |
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Publications |
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Storage |
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin. |
The insulin-like growth factor I receptor (IGF-I R or IGF1R, designated CD221) is a 450 kDa disulfide‑linked heterotetrameric transmembrane glycoprotein consisting of two 130 kDa alpha and two 95 kDa beta subunits (1, 4). The IGF-1 R cDNA encodes a preproreceptor that is proteolytically cleaved to produce the extracellular alpha subunit (amino acid (aa) 31-737), which contains a cysteine-rich region and two ligand‑binding fibronectin type III (FN-III) domains, and the beta subunit (aa 742-1369), which contains an extracellular FN-III domain, transmembrane and cytoplasmic tyrosine kinase domains (1). Extracellular portions of mature mouse IGF-I R share 99.7% aa identity with rat, 96% with human, canine and porcine, and 95% with bovine and equine IGF-I R. IGF-I R is expressed in all cell types and tissues. It binds insulin-like growth factor I (IGF-I) with high affinity, IGF-II with lower affinity, and insulin with lowest affinity (2, 3). Both IGF-I R and the structurally similar insulin receptor (Ins R) activate the same signaling pathways in response to their respective ligands (3). IGF-I R/Ins R hybrids are formed in proportion to their expression and respond primarily to IGF-I, probably down‑regulating cellular response to insulin (2, 5). IGF signaling is also modulated by IGF binding proteins and the scavenger receptor, IGF-II R (4). Expression or glycosylation of IGF-I R may be altered in cancer cells (4, 5). Mice lacking IGF-I R show intrauterine growth deficiency and die at birth due to respiratory failure, and IGF-I R mutations in humans can retarded pre- and postnatal growth (6-8). IGF-I and its receptor are particularly important for neurogenesis, with deficiency producing microcephaly and learning disorders (9-11). Low expression of IGF-I R enhances lifespan in both mouse and human by increasing resistance to oxidative stress (12, 13). IGF-I R expression in human embryonic stem cells is important for their survival and clonogenicity (14).
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