Overview
Product nameIGF1 Receptor protein (Active)See all IGF1 Receptor proteins and peptides ...
Protein descriptionRecombinant fragment, human IGF1 Receptor, cytoplasmic domain (960-end). Expressed by baculovirus in Sf9 insect cells using an N-terminal His tag, 53kDa. Swiss ID = P08069
Expression hostInsect cells
Properties
Purification notesPurity is >75% by densitometry.
Biological activitySpecific activity was 263 nmol /min/mg.
FormLiquid
Storage instructionsShipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.This product is an active protein and may elicit a biological response in vivo, handle with caution.
Storage bufferPreservative: None
Constituents: 25% Glycerol, 50mM Tris HCl, 150mM Sodium chloride, 0.25mM DTT, 0.1mM EGTA, 0.1mM EDTA, 0.1mM PMSF, pH 7.5
Concentration information loading...
Research Areas
Applications
Our Abpromise guarantee covers the use of
ab71657
in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Application
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Notes |
| SDS-PAGE |
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| Functional Studies |
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Application notesKinase assay: Use at an assay dependent dilution. Substrate:IGF1Rtide synthetic peptide (KKKSPGEYVNIEFG) diluted in distilled water to a final concentration of 1mg/ml.
SDS-PAGE: Use at an assay dependent dilution.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
Protein info
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Alternative names
CD221CD221 antigenIGF 1 receptor
IGF 1RIGF I receptorIGF-I receptorIGF1RIGF1R_HUMANIGFIRIGFIRCIGFRInsulin like growth factor 1 receptorInsulin like growth factor 1 receptor precursorInsulin-like growth factor 1 receptor beta chainInsulin-like growth factor I receptorJTK13MGC142170MGC142172MGC18216
see all
FunctionReceptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphorylation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K-driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R.
When present in a hybrid receptor with INSR, binds IGF1. PubMed:12138094 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, PubMed:16831875 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin.
Tissue specificityFound as a hybrid receptor with INSR in muscle, heart, kidney, adipose tissue, skeletal muscle, hepatoma, fibroblasts, spleen and placenta (at protein level). Expressed in a variety of tissues. Overexpressed in tumors, including melanomas, cancers of the colon, pancreas prostate and kidney.
Involvement in diseaseInsulin-like growth factor 1 resistance (IGF1RES) [MIM:270450]: A disorder characterized by intrauterine growth retardation, poor postnatal growth and increased plasma IGF1 levels. Note=The disease is caused by mutations affecting the gene represented in this entry.
Sequence similaritiesBelongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.
Contains 3 fibronectin type-III domains.
Contains 1 protein kinase domain.
Post-translational
modificationsAutophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Autophosphorylation occurs in a sequential manner; Tyr-1165 is predominantly phosphorylated first, followed by phosphorylation of Tyr-1161 and Tyr-1166. While every single phosphorylation increases kinase activity, all three tyrosine residues in the kinase activation loop (Tyr-1165, Tyr-1161 and Tyr-1166) have to be phosphorylated for optimal activity. Can be autophosphorylated at additional tyrosine residues (in vitro). Autophosphorylated is followed by phosphorylation of juxtamembrane tyrosines and C-terminal serines. Phosphorylation of Tyr-980 is required for IRS1- and SHC1-binding. Dephosphorylated by PTPN1.
Polyubiquitinated at Lys-1168 and Lys-1171 through both 'Lys-48' and 'Lys-29' linkages, promoting receptor endocytosis and subsequent degradation by the proteasome. Ubiquitination is facilitated by pre-existing phosphorylation.
Cellular localizationMembrane.
IGF1 Receptor protein (Active) images
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Functional Studies - IGF1 Receptor protein (Active) (ab71657)
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SDS-PAGE - IGF1 Receptor protein (Active) (ab71657)
References for IGF1 Receptor protein (Active) (ab71657)
ab71657
has not yet been referenced specifically in any publications.
Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"
