Cell Signaling Technology

Product Pathways - Metabolism

Phospho-IGF-I Receptor β (Tyr1131)/Insulin Receptor β (Tyr1146) Antibody #3021

igf   igf-1   IGF-1R   IGF-I   IGF-IR   igf1r   Ins-R   InsR   insulin like growth factor 1 receptor   insulin like growth factor I receptor   Insulin-like growth factor 1 receptor   Insulin-like growth factor I receptor   insulin-like-growth-factor   Insulin-receptor   IR  

No. Size Price
3021L 300 µl ( 30 western blots ) ¥8,992.00 现货查询 购买询价
3021S 100 µl ( 10 western blots ) ¥4,050.00 现货查询 购买询价
3021T 20 µl ( 2 western blots ) ¥1,500.00 现货查询 购买询价
3021 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Rat, Endogenous 95 Rabbit
IP 1:50

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting, IP=Immunoprecipitation,


Species predicted to react based on 100% sequence homology: Bovine,

Specificity / Sensitivity

Phospho-IGF-I Receptor β (Tyr1131)/Insulin Receptor β (Tyr1146) Antibody detects endogenous levels of Tyr1131-phosphorylated IGF-I receptor and Tyr1146-phosphorylated insulin receptor. The antibody cross-reacts with activated PDGF, FGF and EGF receptors, ErbB2 and c-Met.

Phospho-IGF-I Receptor β (Tyr1131)/Insulin Receptor β (Tyr1146) 抗体可分别识别内源性的Tyr113磷酸化的IGF-I受体和Tyr1146磷酸化的胰岛素受体。它与激活的PDGF、FGF和EGF受体以及ErbB2和c-Met有交叉反应。

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues of human IGF-I Receptor β. Antibodies are purified by protein A and peptide affinity chromatography.

该多克隆抗体用与人类IGF-I Receptorβ中相应氨基酸序列对应的人工合成肽段免疫动物制成。该抗体使用蛋白A和肽亲和层析纯化而得。

Western Blotting

Western Blotting

Western blot analysis of extracts from 3T3-L1 adipocytes, untreated or insulin-treated (100 nM for the indicated times), using Phospho-IGF-I Receptor β (Tyr1131)/Insulin Receptor β (Tyr1146) Antibody (upper) or control IR antibody (lower).

对3T3-L1脂肪细胞抽提液,未处理或100nM胰岛素处理适当时间,使Phospho-IGF-I Receptor β (Tyr1131)/Insulin Receptor β (Tyr1146) Antibody(上图)或对照IR抗体(下图)进行Western blot分析。

Western Blotting

Western Blotting

Western blot analysis of extracts from 293 cells, untreated or IGF-I-treated (100 nM for 2 minutes), using Phospho-IGF-I Receptor β (Tyr1131)/Insulin Receptor β (Tyr1146) Antibody (upper) or control IGF-I Receptor antibody (lower).

对293细胞抽提液,未处理或100nM IGF-I处理2分钟,使Phospho-IGF-I Receptor β (Tyr1131)/Insulin Receptor β (Tyr1146) Antibody(上图)或对照IGF-I受体抗体(下图)进行Western blot分析。


Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation of Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

I型胰岛素样生长因子受体(IGF-I)是一种跨膜受体酪氨酸激酶,广泛表达于许多细胞系,并在胎儿和产后组织细胞中表达(1-3)。受体与IGF-I和IGF-Ⅱ配体结合后发生自身磷酸化。 激酶结构域的三个酪氨酸残基(Tyr1131,Tyr1135,Tyr1136)是最早确定的三个主要磷酸化位点(4)。三个酪氨酸残基的磷酸化对激酶的活化是必要的(5,6)。胰岛素受体(IR)与IGF-I受体有显著的结构和功能的相似性,都有激酶结构域激活环中对应的酪氨酸残基(Tyr1146/1150/1151)的存在。IR的酪氨酸磷酸化是胰岛素刺激最早的细胞反应之一(7)。自身磷酸化从Tyr1146和Tyr1150或Tyr1151的磷酸化开始,但完全的激酶活性需要三个酪氨酸残基的磷酸化(8)。

  1. Adams, T.E. et al. (2000) Cell Mol Life Sci 57, 1050-93.
  2. Baserga, R. (2000) Oncogene 19, 5574-81.
  3. Scheidegger, K.J. et al. (2000) J Biol Chem 275, 38921-8.
  4. Hernández-Sánchez, C. et al. (1995) J Biol Chem 270, 29176-81.
  5. Lopaczynski, W. et al. (2000) Biochem Biophys Res Commun 279, 955-60.
  6. Baserga, R. (1999) Exp Cell Res 253, 1-6.
  7. White, M.F. et al. (1985) J Biol Chem 260, 9470-8.
  8. White, M.F. et al. (1988) J Biol Chem 263, 2969-80.

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