Key features and details
- Rabbit polyclonal to IGF1 Receptor (phospho Y1161)
- Suitable for: IHC-P, WB, ELISA, IP
- Reacts with: Human
- Isotype: IgG
Product nameAnti-IGF1 Receptor (phospho Y1161) antibody
See all IGF1 Receptor primary antibodies
DescriptionRabbit polyclonal to IGF1 Receptor (phospho Y1161)
SpecificityAb39398 detects endogenous levels of IGF1 Receptor only when phosphorylated at tyrosine 1161.
Tested applicationsSuitable for: IHC-P, WB, ELISA, IPmore details
Species reactivityReacts with: Human
Predicted to work with: Mouse, Rat
- IHC-P: Human breast carcinoma and stomach tissues. WB: HEK-293 treated with insulin cell lysate.
Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Constituents: 50% Glycerol, 0.87% Sodium chloride, PBS
Without Mg2+ and Ca2+
Concentration information loading...
PurityImmunogen affinity purified
Purification notesab39398 was affinity purified from rabbit antiserum by affinity chromatography using an epitope specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using a non-phosphopeptide corresponding to the phosphorylation site.
Our Abpromise guarantee covers the use of ab39398 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|IHC-P||1/50 - 1/100.|
|WB||1/500 - 1/1000. Predicted molecular weight: 155 kDa.|
|IP||Use at an assay dependent concentration.|
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
Sequence similaritiesBelongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.
Contains 4 fibronectin type-III domains.
Contains 1 protein kinase domain.
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. Phosphorylation of Ser-1278 by GSK-3beta restrains kinase activity and promotes cell surface expression, it requires a priming phosphorylation at Ser-1282. 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.
Sumoylated with SUMO1.
Controlled by regulated intramembrane proteolysis (RIP). Undergoes metalloprotease-dependent constitutive ectodomain shedding to produce a membrane-anchored 52 kDa C-Terminal fragment which is further processed by presenilin gamma-secretase to yield an intracellular 50 kDa fragment.
Cellular localizationCell membrane.
- Information by UniProt
- CD221 antibody
- CD221 antigen antibody
- IGF 1 receptor antibody
Western blot analysis using IGF1 Receptor antibody (ab39675, Lane 1, 2 and 3) and IGF1 Receptor (phospho-Tyr1161) antibody (ab39398, Lane 4 and 5).
Immunohistochemical analysis of paraffin-embedded human breast carcinoma tissue using ab39398 diluted 1:50.
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) analysis of human stomach tissue sections labeling IGF1 Receptor (phospho Y1161) with ab39398 at 1/100 dilution. The tissue was fixed with formaldehyde; heat mediated antigen retrieval was performed using a citrate buffer pH 6.0. The tissue was blocked with 5% serum for 1 hour at 23°C followed by incubation with ab39398 at 1/100 for 1 hour at 23°C. An undiluted polyclonal goat anti-rabbit HRP conjugated secondary antibody was used.
Immunohistochemical analysis of paraffin-embedded human breast carcinoma tissue using ab39398 diluted 1:50 after pre-incubation with the immunogen (synthetic phosphopeptide)
ab39398 has been referenced in 45 publications.
- Tian H et al. Effect of Dexmedetomidine-Mediated Insulin-Like Growth Factor 2 (IGF2) Signal Pathway on Immune Function and Invasion and Migration of Cancer Cells in Rats with Ovarian Cancer. Med Sci Monit 25:4655-4664 (2019). PubMed: 31230061
- George B et al. Dual inhibition of IGF-IR and ALK as an effective strategy to eradicate NPM-ALK+ T-cell lymphoma. J Hematol Oncol 12:80 (2019). PubMed: 31340850
- Dong R et al. IGF-1/IGF-1R blockade ameliorates diabetic kidney disease through normalizing Snail1 expression in a mouse model. Am J Physiol Endocrinol Metab 317:E686-E698 (2019). PubMed: 31361542
- Xu Y et al. Down-regulation of SOX18 inhibits laryngeal carcinoma cell proliferation, migration, and invasion through JAK2/STAT3 signaling. Biosci Rep 39:N/A (2019). PubMed: 31189744
- Yan J et al. Downregulation of lncRNA CCDC26 contributes to imatinib resistance in human gastrointestinal stromal tumors through IGF-1R upregulation. Braz J Med Biol Res 52:e8399 (2019). PubMed: 31166382