Anti-IGF1 Receptor (phospho Y1162 + Y1163) antibody (ab5680)

Overview

  • Product nameAnti-IGF1 Receptor (phospho Y1162 + Y1163) antibody
    See all IGF1 Receptor primary antibodies
  • Description
    Rabbit polyclonal to IGF1 Receptor (phospho Y1162 + Y1163)
  • SpecificityAlthough exhibiting a preference for IR/IGF-1R, this antibody has been shown by both peptide competition and protein blotting to react with other dual phosphotyrosine motifs from proteins such as c-Met and Shc.
  • Tested applicationsSuitable for: WBmore details
  • Species reactivity
    Reacts with: Human
    Predicted to work with: Mouse, Rat
  • Immunogen

    Synthetic phosphopeptide derived from the region of Insulin Receptor/IGF1R that contains tyrosines 1162 and 1163. The corresponding residues in the IGF1R are 1135 and 1136.

  • Positive control
    • CHO-T cells transfected with a vector containing insulin receptor and stimulated with 100 nM insulin for 10 minutes at 37°C.

Properties

Applications

Our Abpromise guarantee covers the use of ab5680 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
WB 1/1000. Detects a band of approximately 120 kDa.

Target

  • 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.
  • Post-translational
    modifications
    Autophosphorylated 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
  • Database links
  • Alternative names
    • CD221 antibody
    • CD221 antigen antibody
    • IGF 1 receptor antibody
    • IGF 1R antibody
    • IGF I receptor antibody
    • IGF-I receptor antibody
    • Igf1r antibody
    • IGF1R_HUMAN antibody
    • IGFIR antibody
    • IGFIRC antibody
    • IGFR antibody
    • Insulin like growth factor 1 receptor antibody
    • Insulin like growth factor 1 receptor precursor antibody
    • Insulin-like growth factor 1 receptor beta chain antibody
    • Insulin-like growth factor I receptor antibody
    • JTK13 antibody
    • MGC142170 antibody
    • MGC142172 antibody
    • MGC18216 antibody
    • Soluble IGF1R variant 1 antibody
    • Soluble IGF1R variant 2 antibody
    see all

Anti-IGF1 Receptor (phospho Y1162 + Y1163) antibody images

  • Peptide Competition: Extracts prepared from CHO-T cells transfected with an insulin receptor containing vector and left unstimulated (1) or stimulated with insulin (2-5) were resolved by SDS-PAGE on a 10% polyacrylamide gel and transferred to PVDF. Membranes were blocked with a 5% BSA TBST buffer overnight at 4°C and incubated with the ab5680 antibody for two hours at room temperature in a 3% BSA-TBST buffer, following prior incubation with: no peptide (1, 5), the phosphopeptide immunogen (2), the non-phosphorylated peptide corresponding to the phosphopeptide (3), or, a generic phosphotyrosine containing peptide (4). After washing, membranes were incubated with goat F(ab’)2 anti-rabbit IgG alkaline phosphatase conjugate and bands were detected using the Tropix WesternStar method. The data show that only the phosphopeptide corresponding to IR/IGF1R [pYpY1162/1163] completely blocks the antibody signal, thereby demonstrating the specificity of the antibody. The data also show the activation of the insulin receptor upon stimulation with insulin.

References for Anti-IGF1 Receptor (phospho Y1162 + Y1163) antibody (ab5680)

ab5680 has not yet been referenced specifically in any publications.

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