no metadatahttps://benchmarkantibodies.com/product/biotinylated-human-pdgf-r-beta-cd140b-protein-4738/
Skip to content

Biotinylated Human PDGF R beta/CD140b Protein 4738

$525.00$1,750.00

Summary

  • Expression: HEK293
  • Functional: Yes (ELISA)
  • Amino Acid Range: Leu33-Phe530
Weight1 lbs
Dimensions9 × 5 × 2 in
product tag

C-His-Avi, also biotinylated

Biotinylated Human PDGF R beta/CD140b Protein 4738

protein
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
PDGF is a major serum mitogen that can exist as a homo or hetero-dimeric protein consisting of disulfide-linked PDGF-A and PDGF-B chains. The PDGF-AA,PDGF-BB and PDGF-AB isoforms have been shown to bind to two distinct cell surface PDGF receptors with different affinities. Where as PDGF R alpha binds all three PDGF isoforms with high affinity, PDGF R beta binds PDGF-BB only with high-affinity. PDGF R plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites.
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) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
Gene names
PDGFRB,PDGFRB PDGFR PDGFR1
Protein family
Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamil
Mass
9606Da
Function
FUNCTION: Tyrosine-protein kinase that acts as a 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. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. {ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11331881, ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:1653029, ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:1846866, ECO:0000269|PubMed:20494825, ECO:0000269|PubMed:20529858, ECO:0000269|PubMed:21098708, ECO:0000269|PubMed:21679854, ECO:0000269|PubMed:21733313, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:26599395, ECO:0000269|PubMed:2835772, ECO:0000269|PubMed:2850496, ECO:0000269|PubMed:7685273, ECO:0000269|PubMed:7691811, ECO:0000269|PubMed:7692233, ECO:0000269|PubMed:8195171}.
Catalytic activity
BINDING 606..614; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 634; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000305"
Subellular location
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle. Lysosome lumen. Note=After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation.
Structure
SUBUNIT: Interacts with homodimeric PDGFB and PDGFD, and with heterodimers formed by PDGFA and PDGFB. May also interact with homodimeric PDGFC. Monomer in the absence of bound ligand. Interaction with homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD, leads to receptor dimerization, where both PDGFRA homodimers and heterodimers with PDGFRB are observed. Interacts with SH2B2/APS. Interacts directly (tyrosine phosphorylated) with SHB. Interacts (tyrosine phosphorylated) with PIK3R1 and RASA1. Interacts (tyrosine phosphorylated) with CBL. Interacts (tyrosine phosphorylated) with SRC and SRC family kinases. Interacts (tyrosine phosphorylated) with PIK3C2B, maybe indirectly. Interacts (tyrosine phosphorylated) with SHC1, GRB7, GRB10 and NCK1. Interaction with GRB2 is mediated by SHC1. Interacts (via C-terminus) with NHERF1. {ECO:0000269|PubMed:10454568, ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11567151, ECO:0000269|PubMed:11882663, ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1375321, ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:17620338, ECO:0000269|PubMed:20534510, ECO:0000269|PubMed:2835772, ECO:0000269|PubMed:2850496, ECO:0000269|PubMed:7679113, ECO:0000269|PubMed:7691811, ECO:0000269|PubMed:7692233, ECO:0000269|PubMed:8195171, ECO:0000269|PubMed:8302579, ECO:0000269|PubMed:8940081, ECO:0000269|PubMed:9989826}.
Post-translational modification
PTM: Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-579, and to a lesser degree, at Tyr-581, is important for interaction with SRC family kinases. Phosphorylation at Tyr-740 and Tyr-751 is important for interaction with PIK3R1. Phosphorylation at Tyr-751 is important for interaction with NCK1. Phosphorylation at Tyr-771 and Tyr-857 is important for interaction with RASA1/GAP. Phosphorylation at Tyr-857 is important for efficient phosphorylation of PLCG1 and PTPN11, resulting in increased phosphorylation of AKT1, MAPK1/ERK2 and/or MAPK3/ERK1, PDCD6IP/ALIX and STAM, and in increased cell proliferation. Phosphorylation at Tyr-1009 is important for interaction with PTPN11. Phosphorylation at Tyr-1009 and Tyr-1021 is important for interaction with PLCG1. Phosphorylation at Tyr-1021 is important for interaction with CBL; PLCG1 and CBL compete for the same binding site. Dephosphorylated by PTPRJ at Tyr-751, Tyr-857, Tyr-1009 and Tyr-1021. Dephosphorylated by PTPN2 at Tyr-579 and Tyr-1021. {ECO:0000269|PubMed:10821867, ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:14966296, ECO:0000269|PubMed:15902258, ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:2550144, ECO:0000269|PubMed:7685273}.; PTM: N-glycosylated. {ECO:0000269|PubMed:20534510, ECO:0000269|PubMed:2850496}.; PTM: Ubiquitinated. After autophosphorylation, the receptor is polyubiquitinated, leading to its degradation. {ECO:0000269|PubMed:1313434, ECO:0000269|PubMed:17620338}.
Target Relevance information above includes information from UniProt accession : P09619
The UniProt Consortium

Data

ELISA with Biotinylated Human PDGF R beta/CD140b Protein
Immobilized Anti-PDGF R beta Antibody, hFc Tag at 2µg/ml (100µl/Well) on the plate. Dose response curve for Biotinylated Human PDGF R beta, His Tag with the EC50 of 12.5ng/ml determined by ELISA.
HPLC of Biotinylated Human PDGF R beta/CD140b Protein
The purity of Biotinylated Human PDGF R beta is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Biotinylated Human PDGF R beta/CD140b Protein
Biotinylated Human PDGF R beta on Tris-Bis PAGE under reduced conditions. The purity is greater than 95%.

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.




pmidtitleauthorscitation

Protocols

relevant to this product

Documents

#
No results found

Reviews

There are no reviews yet.

Only logged in customers who have purchased this product may leave a review.