Recombinant Mouse PDGF R beta Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to inhibit the biological activity of PDGF-BB using NR6R-3T3 mouse fibroblast cells. Raines, E.W. et al. (1985) Methods Enzymol. 109:749. The ED 50 for this effect is 6-48 ng/mL in the presence of 4 ng/mL recombinant human PDGF-BB.
Source
Mouse myeloma cell line, NS0-derived mouse PDGF R beta protein
Mouse PDGF R beta (Leu32-Lys530) Accession # P05622
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
82.6 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.
SDS-PAGE
124 kDa, reducing conditions
Publications
Read Publications using 1042-PR in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse PDGF R beta Fc Chimera Protein, CF
The platelet-derived growth factor (PDGF) family consists of proteins derived from four genes (PDGF-A, -B, -C, and -D) that form disulfide-linked homodimers (PDGF-AA, -BB, -CC, and -DD) and a heterodimer (PDGF-AB) (1, 2). These proteins regulate diverse cellular functions by binding to and inducing the homo- or hetero-dimerization of two receptors (PDGF R alpha and R beta ). Whereas alpha / alpha homo-dimerization is induced by PDGF-AA, -BB, -CC, and -AB, alpha / beta hetero-dimerization is induced by PDGF-AB, -BB, -CC, and -DD, and beta / beta homo-dimerization is induced only by PDGF-BB, and -DD (1 - 4). Both PDGF R alpha and R beta are members of the class III subfamily of receptor tyrosine kinases (RTK) that also includes the receptors for M-CSF, SCF and Flt3-ligand. All class III RTKs are characterized by the presence of five immunoglobulin-like domains in their extracellular region and a split kinase domain in their intracellular region. Ligand-induced receptor dimerization results in autophosphorylation in trans resulting in the activation of several intracellular signaling pathways that can lead to cell proliferation, cell survival, cytoskeletal rearrangement, and cell migration. Many cell types, including fibroblasts and smooth muscle cells, express both the alpha and beta receptors. Others have only the alpha receptors (oligodendrocyte progenitor cells, mesothelial cells, liver sinusoidal endothelial cells, astrocytes, platelets and megakaryocytes) or only the beta receptors (myoblasts, capillary endothelial cells, pericytes, T cells, myeloid hematopoietic cells and macrophages). A soluble PDGF R alpha has been detected in normal human plasma and serum as well as in the conditioned medium of the human osteosarcoma cell line MG-63 (5). Both the recombinant mouse and human soluble PDGF R alpha bind PDGF with high affinity and are potent PDGF antagonists.
Betshotz, C. et al. (2001) BioEssays 23:494.
Ostman, A. and A.H. Heldin (2001) Advances in Cancer Research 80:1.
Gilbertson, D. et al. (2001) J. Biol. Chem. 276:27406.
LaRochells, W.J. et al. (2001) Nature Cell Biol. 3:517.
Tiesman, J. and C.E. Hart (1993) J. Biol. Chem. 5:9621.
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