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Insulin Receptor (Thr1160) Antibody

Rabbit Polyclonal Antibody

     
  • WB - Insulin Receptor (Thr1160) Antibody AN1277
    Western blot of HeLa cell lysate showing specific labeling of the ~95 kDa IR protein phosphorylated at Thr1160 in the first lane (-). Phosphospecificity is shown in the second lane (+) where immunolabeling is completely eliminated by blot treatment with lambda phosphatase (λ-Ptase, 1200 units for 30 min).
  • SPECIFICATION
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
WB
Primary Accession P06213
Reactivity Human
Host Rabbit
Clonality Polyclonal
Calculated MW 156333 Da
Additional Information
Gene ID 3643
Gene Name INSR
Target/Specificity Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr1160 conjugated to KLH
Dilution WB~~ 1:1000
Format Antigen Affinity Purified from Pooled Serum
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsInsulin Receptor (Thr1160) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
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Research Areas
Citations (0)

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Background

The insulin receptor (IR) is a well-studied receptor tyrosine kinase composed of two α subunits, responsible for the extracellular insulin binding site, and two β subunits, responsible for intracellular protein kinase activity (Endemann et al., 1990, Chiu et al., 2010). The binding of insulin to the α subunits activates the intrinsic kinase activity located in the β subunits and subsequently initiates a cascade of phosphorylation events causing major conformational changes in the activation loop of the kinase domain, which lead to different biological functions (Chiu et al., 2010). It has been hypothesized that T1160 phosphorylation affects or is affected by Y1158/62/63 phosphorylation and that the conformation of T1160 and pT1160 is likely to be affected by the phosphorylation status of the surrounding tyrosines.

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$ 365.00
Cat# AN1277
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