Recombinant Mouse PDGF R alpha Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit the biological activity of PDGF-AB or PDGF-AA using NR6R‑3T3 mouse fibroblast cells. Raines, E.W. et al. (1985) Methods Enzymol. 109:749. The ED50 for this effect is 0.01-0.04 µg/mL in the presence of 10 ng/mL recombinant human PDGF-AA.
Mouse myeloma cell line, NS0-derived mouse PDGF R alpha protein
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
<0.10 EU per 1 μg of the protein by the LAL method.
82.5 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
125-140 kDa, reducing conditions
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rearranged-in-hypereosinophilia-platelet derived growth factor receptor alphafusion protein
PDGF R alpha (platelet-derived growth factor receptor alpha) is a type I transmembrane glycoprotein in the class III subfamily of receptor tyrosine kinases (RTK) (1-3). PDGF R alpha and PDGF R beta can form homo- or hetero-dimeric receptors when engaged by dimers of the PDGF family of growth factors, which include disulfide-linked homodimers of PDGF-A, B, C or D, or the heterodimer PDGF-AB that is mainly found in human platelets. While multiple in vitro ligand-receptor combinations have been identified, in vivo evidence indicates that PDGF R alpha primarily binds PDGF-AA and PDGF-CC, while PDGF R beta primarily binds PDGF-BB and probably PDGF-DD. Like all class III RTKs, the extracellular domain (ECD) of mouse PDGF R alpha (amino acids 25-525) contains five immunoglobulin-like domains, while the intracellular region contains a split tyrosine kinase domain (aa 593‑954). Within the ECD, mouse PDGF R alpha shares 85%, 93%, 84%, 84%, and 81% amino acid sequence identity with human, rat, equine, canine and bovine PDGF R alpha respectively. PDGF R alpha autophosphorylates upon dimerization, activating signaling cascades in PI 3-kinase Ras-MAP kinase, and PLC-gamma pathways (1, 2). Signaling is down‑regulated by SHP-2 phosphatase activity and by receptor endocytosis and lysosomal degradation. PDGF R alpha is expressed at low levels in most mesenchymal cells, but is strongly expressed in oligodendrocyte, lung, skin and intestinal progenitor cells and induced by inflammation or growth in culture (1-3). During development, mesenchymal cells expressing PDGF R alpha respond to local gradients of epithelially produced PDGF-AA or PDGF-CC during formation of the cranial and cardiac neural crest, retina, gonads, lung alveoli, intestinal villi, skin, hair follicles, skeleton, teeth, palate, and interstitial kidney mesenchyme (1, 4). Deletion of PDGF R alpha in mice severely impairs mesenchymal derivatives in both embryo and extraembryonic tissues, and high or low PDGF R alpha signaling in humans may result in spina bifida or cleft palate‑type malformations. Postnatally, PDGF R alpha is implicated in gliomas and fibrotic disorders of lung, heart and skin (scleroderma) (5- 7).
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Baroni, S.S. et al. (2006) N. Engl. J. Med. 354:2667.
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