Recombinant Rat PDGF R beta His-tag Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Rat PDGF-BB
(Catalog #
520-BB/CF)
is coated at 2 µg/mL (100 μL/well), Recombinant Rat PDGF R beta His-tag binds with an ED 50 of 0.04-0.2 μg/mL. |
Source |
Mouse myeloma cell line, NS0-derived rat PDGF R beta protein Leu32-Lys530, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Leu32 |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
57 kDa. 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 |
88-102 kDa, under reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Rat PDGF R beta His-tag Protein, CF
Background
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
heterodimerization 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 ~123 kDa 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. The extracellular domain of rat PDGF R beta contains 4 disulfide bonds and
shares a 79.2% and 96.6% sequence identity with human and mouse PDGF R beta ,
respectively. 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. PDGF R alpha is also expressed on the
Golgi Apparatus and PDGF R beta is expressed on lysosomes. 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). 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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