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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Phospho-IRS-1 (Ser318) (D51C3) Rabbit mAb #5610

Filter:
  • WB
  • IP
Western Blotting Image 1: Phospho-IRS-1 (Ser318) (D51C3) Rabbit mAb
Western blot analysis of extracts from serum-starved C2C12 cells, untreated or insulin-treated (150 nM for 5 min.), using Phospho-IRS-1 (Ser318) (D51C3) Rabbit mAb (upper), or IRS-1 Antibody #3407 (lower).

To Purchase # 5610

Cat. # Size Qty. Price
5610T 20 µl
$173
5610S 100 µl
$401

Supporting Data

REACTIVITY H M
SENSITIVITY Endogenous
MW (kDa) 180
Source/Isotype Rabbit IgG
Application Key:
  • WB-Western Blotting 
  • IP-Immunoprecipitation 
Species Cross-Reactivity Key:
  • H-Human 
  • M-Mouse 
  • Related Products

Product Information

Product Usage Information

Application Dilution
Western Blotting 1:1000
Immunoprecipitation 1:50

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

Phospho-IRS-1 (Ser318) (D51C3) Rabbit mAb recognizes endogenous levels of IRS-1 protein only when phosphorylated at Ser318. Note: Ser318 is the mouse residue; the corresponding human residue is Ser323. The antibody cross reacts with a inducible nonspecific band at around 57 kDa.

Species Reactivity:

Human, Mouse

The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

Species predicted to react based on 100% sequence homology:

Rat

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser318 of mouse IRS-1 protein.

Background

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).
PKC phosphorylates mouse IRS-1 at Ser318 (human Ser323) by insulin receptor activation or by other stimulation such as TPA, IL-6, retinoic acid treatment (11-14) . The phosphorylation at Ser318 acts as a negative feedback signal to down regulates of insulin effect (14-16).
  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. Greene, M.W. et al. (2004) Biochem J 378, 105-116.
  12. Weigert, C. et al. (2006) J Biol Chem 281, 7060-7067.
  13. del Rincón, S.V. et al. (2004) Oncogene 23, 9269-9279.
  14. Moeschel, K. et al. (2004) J Biol Chem 279, 25157-25163.
  15. Weigert, C. et al. (2005) J Biol Chem 280, 37393-37399.
  16. Hennige, A.M. et al. (2006) FASEB J 20, 1206-1208.

Pathways

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