| Cat.# |
CB4378
|
| Size |
76
µg / 200
ml |
| Isotype:
|
rabbit polyclonal
IgG
|
| Epitope: |
synthetic
peptide containing human insulin receptor sequence (854-966)
which includes phosphorylated Tyr960
|
|
Species
&
specficity:
|
Anti-Phospho-Insulin
Receptor (Tyr960) specifically
detects endogenous levels of phosphorylated insulin receptor-b
protein.
The molecular weight of detected insulin receptor-b
is 97 kDa. This antibody does not cross-react with other IR-family
members.
|
| Storage: |
Store
at -20°C, 4°C for frequent use. Avoid repeated freeze-thaw
cycles.
|
| MW:
|
97
kDa
|
|
Application:
|
IHC
(Paraffin)
|
IP |
WB
|
| Dilution:
|
1:50 |
1:50 |
1:1000
|
|
Background:
Insulin
receptor is a
transmembrane receptor that is activated by insulin. It belongs to the
large class of tyrosine kinase receptors. Two alpha subunits and two
beta subunits make up the insulin
receptor. The beta subunits pass through the cellular membrane
and are linked by disulfide bonds1. Insulin receptor
functions as an enzyme that transfers phosphate groups from ATP to
tyrosine residues on intracellular target proteins. Binding of insulin
to the alpha subunits causes the beta subunits to phosphorylate
themselves (autophosphorylation), thus activating the catalytic activity
of the receptor. The activated receptor then phosphorylates a number of
intracellular proteins, which in turn alters their activity, thereby
generating a biological response2.
Several
intracellular proteins have been identified as phosphorylation
substrates for the insulin receptor, the best-studied of which is insulin
receptor substrate 1 or IRS-1. The juxtamembrane phosphorylation
site Tyr960 within the insulin receptor cytoplasmic domain is an
essential determinant for the tyrosine phosphorylation of
IRS-15. When
IRS-1 is activated by phosphorylation, it serves as a type of docking
center for recruitment and activation of other enzymes that ultimately
mediate insulin's effects, including activation of PI-3-kinase and MAP
kinase pathways3,4.
References:
1.
Youngren, J.F.: Cell
Mol Life Sci. 64:873, 2007.
2.
Backer, J.M. et
al. J Cell Biol.118:831,
1992.
3.
Sesti, G. : Best
Pract Res Clin Endocrinol Metab. 20:665, 2006.
4.
Gual, P. et al. : Biochimie 87:99, 2005.
5.
Backer, J.M. et al. J Cell Biol. 118:831, 1992.
|
|
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