Recombinant Human PDGF R beta His-tag Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human PDGF R beta His-tag protein is immobilized at 0.5 µg/mL (100 µL/well), Recombinant Human PDGF-BB
(Catalog #
220-BB)
binds with an ED 50 of 0.5-3 ng/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human PDGF R beta protein Leu33-Lys531, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Leu33 |
Structure / Form |
Monomer |
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 |
93-103 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 Human 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 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 human PDGF R beta contains 4 disulfide
bonds and shares a 79% sequence identity with mouse and rat PDGF R beta. 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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