Recombinant Human PDGF R beta His-tag Avi-tag Protein, CF New
Recombinant Human PDGF R beta His-tag Avi-tag Protein, CF Summary
Product Specifications
Leu33-Lys531, With a C-terminal 6-His tag & Avi-tag
Analysis
Product Datasheets
Carrier Free
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.
AVI10676
Formulation | Supplied as a 0.2 μm filtered solution in PBS. |
Shipping | The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles. |
Scientific Data
Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human PDGFR beta His-tag Avi-tag Protein (Catalog # AVI10676) binds to Recombinant Human PDGF-BB Protein (220-BB) with an ED50 of 0.150-1.50 μg/mL.
2 μg/lane of Biotinylated Recombinant Human PDGF R beta His-tag Avi-tag Protein (Catalog # AVI10676) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 100-110 kDa, under reducing conditions.
Reconstitution Calculator
Background: PDGF R beta
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. Our Avi-tag Biotinylated human PDGF R beta features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
- 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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