| Cat.# |
CB0218
|
| Size |
90
µg /
200 ml |
| Isotype:
|
rabbit
polyclonal IgG
|
| Epitope: |
E.
coli-expressed
recombinant human IRS-1 protein fragments. |
|
Species
&
specficity:
|
Anti-IRS-1
antibody specifically detects endogenous levels of IRS-1
proteins.
Anti-IRS-1
reacts with human, mouse, & rat IRS-1. Anti-IRS-1 does not
cross-react with other IRS-family members.
|
| Storage: |
-20°
|
| MW:
|
180
kDa
|
|
Application:
|
WB
|
IP |
| Dilution:
|
1:1000
|
1:50 |
|
Background:
Insulin
receptor substrate (IRS) proteins play a central role in maintaining
basic cellular functions such as growth and metabolism. IRS proteins act
as an interface between multiple growth factor receptors possessing
tyrosine kinase activity, such as the insulin receptor, and a complex
network of intracellular signaling molecules containing Src homology 2
(SH2) domains. Four members (IRS-1, IRS-2, IRS-3, IRS-4) of this family
have been identified which differ in their subcellular distribution and
interaction with SH2 domain proteins1. Insulin receptor
substrate-1 (IRS-1) is a major substrate of insulin and insulin-like
growth factor-I receptors. The activated insulin receptor phosphorylates
the intracellular substrate IRS-1, which then binds various signaling
molecules that contain SH2 domains, thereby propagating the insulin
signal. Among these IRS-1-binding proteins, the Grb2-Sos complex and the
protein tyrosine phosphatase SHP-2 transmit mitogenic signals through
the activation of Ras, and phosphoinositide 3-kinase is implicated in
the major metabolic actions of insulin2. Insulin also
activates several kinases that induce the phosphorylation of IRS-1 on
specific serine/ threonine sites and inhibit its functions. This is part
of the negative-feedback control mechanism induced by insulin that leads
to termination of its action3. Agents which induce insulin
resistance, such as free fatty acids, cytokines, angiotensin II,
endothelin-1, amino acids, cellular stress and hyperinsulinemia, also
lead to activation of several serine/threonine kinases and
phosphorylation of IRS-1. These agents negatively regulate IRS-1
function by phosphorylation and other molecular mechanisms (SOCS
expression, IRS degradation, O-linked glycosylation)4.
IRS-1
mediates the control of various cellular processes by insulin.
References:
1.Yenush,
L. & White, M.F. : Bioessays 19:491, 1997. 2.
Ogawa, W., Matozaki, T., & Kasuga, M. : Mol. Cell. Biochem. 182:13,
1998. 3.
Sesti,
G. : Best Pract Res Clin Endocrinol Metab. 20:665, 2006. 4.
Gual,
P. et al. : Biochimie 87:99, 2005.
|
|
Specific
detection of IRS-1 proteins from various cell lysates in Western blot
analysis using IRS-1
rabbit polyclonal antibody.
|
