| Cat.# |
CB5796
|
| Size |
130 µg / 200
ml |
| Isotype:
|
rabbit polyclonal
IgG
|
| Epitope: |
Synthetic
peptide containing phospho-Tyr751 of human PDGF receptor-beta
sequence (746-758).
|
|
Species
&
specficity:
|
Human,
mouse, & rat PDGFR-b.
Anti-Phospho-PDGFR-b
(Tyr751) specifically
detects endogenous levels of PDGF receptor-b
proteins
phosphorylated at Tyr751. This
antibody does not cross-react with other PDGFR-family members.
|
| Storage: |
Store
at -20°C, 4°C for frequent use. Avoid repeated freeze-thaw
cycles.
|
| MW:
|
190
kDa
|
|
Application:
|
IHC
(Paraffin)
|
WB
|
| Dilution:
|
1:50 |
1:1000
|
|
Background:
Platelet-derived
growth factor (PDGF) acts as a potent mitogen, chemoattractant and
survival factor for mesenchymal cells. In addition to its importance in
mammalian development, PDGF plays a critical role in physiological
repair mechanisms and in the pathogenesis of various proliferative
diseases1. The biological effects of PDGF are initiated via
two related receptor tyrosine kinases, termed alpha and beta PDGF
receptors. There are three PDGF isoforms, denoted PDGF-AA, -AB, and -BB,
which are homo- or heterodimers of related A and B polypeptide chains.
The PDGFR-b
binds
only B-chain-containing PDGF isoforms, PDGF-BB binds with high affinity (ICd,
0.5 m) and PDGF-AB with lower affinity (Kd, 2.5 m), but there
is no appreciable affinity for PDGF-AA. The
a-receptor
binds all three PDGF isoforms with similar affinities (Kd, 0.1-0.5
nM). The receptors are structurally related transmembrane glycoproteins
and form, together with CSF-1 receptor, Flt3, and c-Kit, a subfamily
within the superfamily of tyrosine kinases2. Binding of PDGF
induces dimerization of the receptors in vitro and in vivo.
PDGF-AA induces PDGFR
a-a
homodimers,
PDGF-AB induces PDGFR a-a
homodimers
and a-b
heterodimers,
and PDGF-BB induces all three types (a-a,
a-b,
and
b-b)
of
dimers. Dimerization is accompanied by, and might be a prerequisite for
activation of the kinase. Kinase activation is visualized as tyrosine
phosphorylation of the receptor molecules, known as autophosphorylation.
Tyrosine phosphorylation sites in PDGFR, as with other RTKs, serve two
purposes: (i) to control the state of activity of the kinase and (ii) to
create binding site for downstream signal transduction molecules, which
in many cases also are substrates for the kinase3.
Phosphorylation of the PDGF receptor-b
at
Tyr751 forms a docking site for PI 3-kinase4. The activities
of the signaling components are ultimately manifested as specific
biological responses.
References:
1.
Fredriksson, L et al.:
Cytokine Growth Factor Rev. 15:197, 2004.
2.
Tallquist, M. & Kazlauskas, A.:
Cytokine Growth Factor Rev. 15:205, 2004.
3.
Funa, K. & Uramoto,
H.: Acta Biochim Pol. 50:647, 2003.
4.
Li, H.Y. et al.: FEBS
Lett. 540:106, 2003.
|
|
|
Specific
detection of PDGF receptor-b proteins containing
phosphorylated Tyr751 from human skeletal muscle cells stimulated with
PDGF-BB in Western blot
analysis using phospho- PDGF receptor-b
(Tyr751) rabbit polyclonal antibody.
|
|