| Cat.# |
CB4736
|
| Size |
178
µg / 200
ml |
| Isotype:
|
rabbit polyclonal
IgG
|
| Epitope: |
E.
coli-expressed
cytoplasmic domain of human PDGF receptor-b.
|
|
Species
&
specficity:
|
Human,
mouse, & rat PDGFR-b.
Anti-PDGFR-b
specifically
detects endogenous levels of PDGF receptor-b.
The molecular weight of detected PDGF receptor-b
is
190 kDa. 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:
|
97
kDa
|
|
Application:
|
IHC
(Paraffin)
|
IP |
WB
|
FACS |
| Dilution:
|
1:50 |
1:50 |
1:1000
|
1:50 |
|
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. 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.
|
|
Specific
detection of PDGF receptor-b
proteins from human
skeletal muscle cell lysates (lane 1) and adipocyte lysates
(lane 2) in Western blot analysis using PDGF
receptor-b
rabbit polyclonal antibody.
|
