IRS-1 (pS312)
Insulin receptor substrate 1; IRS1

PDF Image Download Product PDF
Product Preparation
A synthetic peptide corresponding to the epitope ATSPA with a single phosphorylation site Ser 312 of human IRS-1.
Background
Insulin Receptor Substrate-1 (IRS-1), 165 kDa cytoplasmic docking protein, is one of the major endogenous substrates of the insulin receptor kinase. IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2 domain containing proteins, which mediate the metabolic and growth promoting functions of insulin. IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser312 of IRS-1 is phosphorylated by JNK and IKK and Ser789 is phosphorylated by SIK-2, a member of AMPK family. The phosphorylation of Tyr612 and Ser636/639 is mediated by the PKC and mTOR pathways, respectively and phosphorylation at Ser1101 is mediated by PKC, resulting in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity.
PURIFICATION
The Rabbit IgG is purified by site-modified Epitope Affinity Purification.
SPECIFICITY
This antibody recognizes ~165 kDa of human IRS-1 (pSer312). It also reacts with mouse and rat. The other species are not tested.
FORMULATION
This affinity purified antibody is supplied in sterile Tris-buffered saline (pH7.2) containing antibody stabilizer.
STORAGE
The antibodies are stable for 12 months from date of receipt when stored at –20oC. The antibodies can be stored at 2oC-8oC for one month without detectable loss of activity. Avoid repeated freezing-thawing cycles.
Gene ID
3667
Applications/Suggested Working Dilutions
Western Blot
0.1-1 µg/ml
ELISA
0.01-0.1 µg/ml
Immunoprecipitation
2-5 µg/ml
IHC
2-10 µg/ml
Flow cytometry
5-10 µg/ml
Order Info
Catalog #: 500-8984
Lot #: See the label
Size: 100 ug
Host: Rabbit
Isotyping: Rabbit IgG
Applications: WB, IP
Reactivity: Hu/Rt/Ms
Price: $ 295.00
REFERENCES
Li, Y. et al. (2004) J. Biol. Chem. 279, 45304–45307.
©2011-2015 Abbomax.com. All rights reserved.