Cell Signaling Technology

Product Pathways - Metabolism

Phospho-IRS-1 (Ser302) Antibody #2384

Insulin Receptor Substrate 1   insulin-receptor   insulin-receptor-substrate   IRS 1   IRS-1   IRS1   rtkscaffold  

No. Size Price
2384S 100 µl ( 10 western blots ) ¥3,900.00 现货查询 购买询价
2384 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Rat, Endogenous 180 Rabbit

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting,


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

Specificity / Sensitivity

Phospho-IRS-1 (Ser 302) Antibody detects endogenous levels of IRS-1 only when phosphorylated at Ser302 of mouse IRS-1 or Ser307 of human IRS-1. This antibody does not detect IRS-1 phosphorylated at other sites.

Phospho-IRS-1 (Ser 302)抗体识别内源性的Ser302磷酸化的鼠IRS-1或Ser307磷酸化的人IRS-1。此抗体不与其它部位磷酸化的IRS-1蛋白发生交叉反应。

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser 302 of mouse IRS-1. Antibodies are purified by protein A and peptide affinity chromatography.


Western Blotting

Western Blotting

Western blot analysis of extracts from CHO IR/IRS-1 cells ( transfected with insulin receptor and IRS-1), untreated or insulin-treated (100 nM for 5 min), showing an increase in phospho-IRS-1 (Ser302) with insulin stimulation, using Phospho-IRS1 (Ser302) Antibody. To confirm phospho-specificity of the antibody, a duplicate membrane was treated with calf intestinal alkaline phosphatase (CIP) after Western transfer.

对CHO IR/IRS-1细胞(转染胰岛素受体和IRS-1)抽提液,未处理或100nM胰岛素处理5分钟,使用Phospho-IRS1 (Ser302) Antibody进行Western blot分析,显示胰岛素刺激后phospho-IRS-1 (Ser302)水平上升。抗体磷酸化特异性由western转膜后对副本膜进行小牛肠碱性磷酸酶(CIP)处理验证。


Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

胰岛素受体底物1(IRS-1)是胰岛素受体激酶的主要底物之一(1)。IRS-1包括多个酪氨酸磷酸化模体,作为与包含SH2结构域的蛋白质的接合位点,介导胰岛素的代谢和生长促进功能(2-4)。IRS-1也包含超过30个潜在的丝氨酸/苏氨酸磷酸化位点。JNK(5)和IKK(6)对IRS-1 Ser307位点进行磷酸化,SIK2(AMPK家族成员之一)对Ser789进行磷酸化(7)。PKC和mTOR途径分别介导IRS-1的Ser612和Ser636/639磷酸化(8,9)。IRS-1在Ser1101的磷酸化由PKCθ介导,可以导致细胞内胰岛素信号通路的抑制,这暗示其在某些肥胖模型中的胰岛素抵抗机制中发挥作用(10)。

Ser302 in rat/mouse IRS-1 (corresponding to Ser307 of human IRS-1) is phosphorylated rapidly during insulin stimulation and has a postive role in IRS-1 tyrosine phosphorylation. Inhibition of Ser302 phosphorylation by short-term amino acid/glucose starvation correlates with a decrease in IRS-1 tyrosine phosphorylation without inhibition of insulin receptor autophosphorylation or Akt phosphorylation. A defect in this positive regulatory pathway may be a mechanism contributing to insulin resistence (11).


  1. Sun, X.J. et al. (1991) Nature 352, 73-77.
  2. Sun, X.J. et al. (1992) J. Biol. Chem. 267, 22662-22672.
  3. Myers Jr., M.G. et al. (1993) Endocrinology 132, 1421-1430.
  4. Wang, L.M. et al. (1993) Science 261, 1591-1594.
  5. Rui, L. et al. (1997) J. Clin. Invest. 107, 181-189.
  6. Gao, Z. et al. (2002) J. Biol. Chem. 277, 48115-48121.
  7. Horike, N. et al. (2003) J. Biol. Chem. 278, 18440-18447.
  8. Ozes, O.N. et al. (2001) Proc. Natl. Acad. Sci. USA 98, 4640-4645.
  9. De Fea, K. and Ruth, R.A. (1997) Biochemistry 36, 12939-12947.
  10. Li, Y. et al. (2004) J. Biol. Chem. 279, 45304-45307.
  11. White, M. F. et al. (2004) J. Biol. Chem. 279, 3447-3454.

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