Cell Signaling Technology

Product Pathways - Tyrosine Kinase/ Adaptors

Platelet-Derived Growth Factor (PDGF) #9909

MW Source Purity
29 kDa Human Recombinant Protein

Description

The human PDGF-B coding cDNA was obtained from hepatocytic mRNA, subcloned into an expression vector and expressed in yeast. The recombinant human PDGF-BB dimmer was purified and stored in PBS buffer containing 0.1% BSA.

Concentration and Specific Activity

100 µg/ml

Western Blotting

Western Blotting

Western blot analysis of extracts from NIH/3T3 cells, untreated or PDGF-stimulated (50 ng/ml for 5 minutes), using Phospho-PDGF Receptor beta (Tyr751) Antibody #3161 (upper) or PDGF receptor beta antibody (lower).

Directions for Use

CST recommends using 50-100 ng/ml of PDGF for stimulation of PDGF signaling.

Background

Platelet-derived growth factor (PDGF) is a dimeric molecule that exists in homodimers or heterodimers of related polypeptide chains (A and B). Two types of PDGF receptors have been identified. The PDGF alpha-receptor binds all three PDGF isoforms with high affinity, whereas the beta-receptor binds only PDGF-BB with high affinity, PDGF-AB with low affinity and does not appear to bind PDGF-AA (1). Ligand binding induces receptor dimerization and autophosphorylation, allowing binding and activation of cytoplasmic SH2-domain-containing signal transduction molecules. A number of different signaling pathways are then initiated, leading to cell growth, actin reorganization, migration and differentiation (2-4). In clinical studies, PDGF expression has been demonstated in a number of different solid tumors, from glioblastomas to prostate carcinomas. In these various tumor types, the biological role of PDGF signaling can vary from autocrine stimulation of cancer cell growth to more subtle paracrine interactions involving adjacent stroma and even angiogenesis. Targeting PDGF signaling is becoming an effective way for tumor treatment (5).

  1. Westermark, B. et al. (1990) Ciba Found. Symp. 150, 6-22.
  2. Heldin, C.H. (1997) FEBS Lett. 410, 17-21.
  3. Bornfeldt, K.E. et al. (1995) Ann. N.Y. Acad. Sci. 766, 416-430.
  4. Renhowe, P.A. (2002) Curr. Opin. Drug Discov. Devel. 5, 214-224.
  5. George, D. (2001) Semin. Oncol. 28, 27-33.

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