» Sign in / Register

PDGFR-βGST - cytosolic region

Platelet-derived growth factor receptor

human, recombinant, Sf9 insect cells

Cat. No. Amount Price (EUR) Buy / Note
PR-357 20 μg 223,96 Add to Basket/Quote Add to Notepad

For in vitro use only!

Shipping: shipped on dry ice

Storage Conditions: store at -80 °C
avoid freeze/thaw cycles

Shelf Life: 12 months

Accession number: NM_002609

Accession number: NM_002609

Purity: > 90 % (SDS-PAGE)

Form: liquid (Supplied in 50 mM Tris-HCl pH 8.0, 100 mM NaCl and 1 mM DTT)

Activity: 3 units/μg (1 unit is defined as transfer of 1 pmol phosphate to the substrate peptide KKKSKDESVDYVPMLDMKG per minute at 30°C).

Platelet-derived growth factors (PDGF) are potent mitogens for cells of mesenchymal origin, including smooth muscle cells and glial cells. The PDGF isoforms AA, BB, AB, CC, and DD are dimeric molecules. They bind two receptor molecules simultaneously and dimerize them upon binding. There are two PDGF receptor isoforms. The α-receptor binds the A, B, and C chains of PDGF with high affinity, whereas the β-receptor binds the B and D chain with high affinity. α- and β-receptor homodimers as well as αβ-receptor heterodimers can transduce mitogenic signals. Aberrant activation of PDGF receptors has been linked with different malignancies as well as with pathological proliferation of fibroblasts or smooth muscle cells in the context of fibrosis and atherosclerosis. The autophosphorylation induced after dimerization of PDGF receptors serves two important functions. On one hand, phosphorylation of a conserved tyrosine residue inside the kinase domains (Tyr-849 in the α,-receptor and Tyr-857 in the β-receptor) leads to an increase in the catalytic efficiencies of the kinase. On the other hand, autophosphorylation of tyrosine residues located outside the kinase domain creates docking sites for signal transduction molecules containing SH2 domains, e.g. PI3-kinase (Cat.# PR-341), PLC-γ, Src (Cat.# PR-900), SHP-2, Ras-GAP (Cat.# PR-223), and Stat5. The GST-Tag facilitates the protein`s application in typical GST pull-down assays.

Selected References:
Claesson-Welsh et al. (1988) cDNA cloning and expression of a human platelet-derived growth factor (PDGF) receptor specific for Bchain- containing PDGF molecules. Mol. Cell. Biol. 8:3476.
Heldin et al. (1999) Mechanism of Action and In Vivo Role of Platelet-Derived Growth Factor. Physiol. Rev. 79:1283.
Kovalenko et al. (1997) Phosphorylation site-specific inhibition of platelet-derived growth factor β-receptor autophosphorylation by the receptor blocking tyrphostin AG1296 Biochemistry 36:6260.
Heldin et al. (2002) New members of the platelet-derived growth factor family of mitogens. Arch. Biochem. Biophys. 398:284.
Pietras et al. (2003) PDGF receptors as cancer drug targets. Cancer Cell. 3:439.