Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | A0A2K5TUS0 |
express system | HEK293 |
product tag | C-His |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
background | Platelet-derived growth factor receptor (PDGFR) signaling is involved in proliferation and survival in a wide array of cell types.PDGFR-β signalling, via TGF-β signalling, may be crucial for restoration of BBB integrity after cerebral ischemia and therefore represents a novel potential therapeutic target. |
molecular weight | The protein has a predicted MW of 57.49 kDa. Due to glycosylation, the protein migrates to 75-105 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Cynomolgus PDGF R beta/CD140b Protein 3119
$300.00 – $1,000.00
Summary
- Expression: HEK293
- Functional: Yes (ELISA)
- Amino Acid Range: Leu33-Lys531
Cynomolgus PDGF R beta/CD140b Protein 3119
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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Platelet-derived growth factor receptor (PDGFR) signaling is involved in proliferation and survival in a wide array of cell types.PDGFR-β signalling, via TGF-β signalling, may be crucial for restoration of BBB integrity after cerebral ischemia and therefore represents a novel potential therapeutic target. |
Protein names Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) |
Gene names PDGFRB,PDGFRB |
Protein family Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamil |
Mass 9541Da |
Function Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. |
Catalytic activity BINDING 579; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000256|PIRSR:PIRSR000615-3"; BINDING 606..614; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000256|PIRSR:PIRSR500948-2"; BINDING 607..614; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000256|PIRSR:PIRSR000615-2"; BINDING 634; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000256|PIRSR:PIRSR000615-2, ECO:0000256|PROSITE-ProRule:PRU10141"; BINDING 682..688; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000256|PIRSR:PIRSR000615-2"; BINDING 830; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000256|PIRSR:PIRSR000615-2"; BINDING 831; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000256|PIRSR:PIRSR000615-3"; BINDING 844; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000256|PIRSR:PIRSR000615-3" |
Subellular location Cell membrane ; Single-pass type I membrane protein. Cytoplasmic vesicle. Lysosome lumen. Membrane ; Single-pass type I membrane protein . |
Structure Interacts with homodimeric PDGFB and PDGFD, and with heterodimers formed by PDGFA and PDGFB. |
Target Relevance information above includes information from UniProt accession: A0A2K5TUS0 |
The UniProt Consortium |
Data
Publications
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.pmid | title | authors | citation |
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Protocols
relevant to this product |
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Documents
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