Recombinant Human PDGF R alpha Protein, CF
Recombinant Human PDGF R alpha Protein, CF Summary
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 100 μg/mL in sterile PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Background: PDGF R alpha
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) (1‑4). 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 human PDGF R alpha (aa 24‑524) contains five immunoglobulin-like domains, while the intracellular region contains a split tyrosine kinase domain (aa 593‑954) (1‑4). Within the ECD, human PDGF R alpha shares 85%, 83%, 95%, 93%, and 88% aa sequence identity with mouse, 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 (1‑4). 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, 5). 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) (6‑8).
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- Klinghoffer, R.A. et al. (2002) Dev. Cell 2:103.
- Martinho, O. (2009) Br. J. Cancer 101:973.
- Olson, L.E. and P. Soriano (2009) Dev. Cell 16:303.
- Baroni, S.S. et al. (2006) N. Engl. J. Med. 354:2667.
Citations for Recombinant Human PDGF R alpha Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 3
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Discovery of High-Affinity PDGF-VEGFR Interactions: Redefining RTK Dynamics
Authors: SB Mamer, S Chen, JC Weddell, A Palasz, A Wittenkell, M Kumar, PI Imoukhuede
Sci Rep, 2017;7(1):16439.
Sample Types: Recombinant Protein
Applications: Surface Plasmon Resonance
Binding of CD157 protein to fibronectin regulates cell adhesion and spreading.
Authors: Morone S, Augeri S, Cuccioloni M, Mozzicafreddo M, Angeletti M, Lo Buono N, Giacomino A, Ortolan E, Funaro A
J Biol Chem, 2014;289(22):15588-601.
Sample Types: Protein
Inhibition of receptor signaling and of glioblastoma-derived tumor growth by a novel PDGFRbeta aptamer.
Authors: Camorani S, Esposito C, Rienzo A, Catuogno S, Iaboni M, Condorelli G, de Franciscis V, Cerchia L
Mol Ther, 2014;22(4):828-41.
Sample Types: Whole Cells
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