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Biotinylated Human PDGF R alpha/PDGFRA Protein 4719



  • Expression: HEK293
  • Functional: Yes (ELISA)
  • Amino Acid Range: Gln24-Glu524
Weight1 lbs
Dimensions9 × 5 × 2 in
product tag

C-His-Avi, also biotinylated

Biotinylated Human PDGF R alpha/PDGFRA Protein 4719

Size and concentration
100, 500µg and 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.
> 95% as determined by Tris-Bis PAGE
target relevance
Platelet-derived growth factor is commonly known as a mitogen. Many research data suggest a role for PDGF-beta R in the mitogenic response of mesangial cells. There are four members of PDGF family known as PDGF-A chain, PDGF-B chain, PDGF-C chain and PDGF-D chain, which in active forms are dimers. As far as two receptors PDGF-alpha R and PDGF-beta R are known to bind PDGF.
Protein names
Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (CD140a antigen) (Platelet-derived growth factor alpha receptor) (Platelet-derived growth factor receptor 2) (PDG
Gene names
Protein family
Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamil
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -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 PIK3R1, PLCG1, and PTPN11. 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. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. 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:10734113, ECO:0000269|PubMed:10947961, ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:12522257, ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:17087943, ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:17141222, ECO:0000269|PubMed:20972453, ECO:0000269|PubMed:21224473, ECO:0000269|PubMed:21596750, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664, ECO:0000269|PubMed:8760137, ECO:0000269|PubMed:8943348}.
Catalytic activity
BINDING 599..607; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"; BINDING 627; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
Subellular location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14644164, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664}; Single-pass type I membrane protein {ECO:0000269|PubMed:14644164, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664}. Cell projection, cilium {ECO:0000250|UniProtKB:P26618}. Golgi apparatus {ECO:0000250|UniProtKB:P26618}.
TISSUE SPECIFICITY: Detected in platelets (at protein level). Widely expressed. Detected in brain, fibroblasts, smooth muscle, heart, and embryo. Expressed in primary and metastatic colon tumors and in normal colon tissue. {ECO:0000269|PubMed:2536956, ECO:0000269|PubMed:7896447, ECO:0000269|PubMed:8188664}.
SUBUNIT: Interacts with homodimeric PDGFA, PDGFB and PDGFC, and with heterodimers formed by PDGFA and PDGFB. Monomer in the absence of bound ligand. Interaction with dimeric PDGFA, PDGFB and/or PDGFC leads to receptor dimerization, where both PDGFRA homodimers and heterodimers with PDGFRB are observed. Interacts (tyrosine phosphorylated) with SHB (via SH2 domain) (By similarity). Interacts (tyrosine phosphorylated) with SHF (via SH2 domain). Interacts (tyrosine phosphorylated) with SRC (via SH2 domain). Interacts (tyrosine phosphorylated) with PIK3R1. Interacts (tyrosine phosphorylated) with PLCG1 (via SH2 domain). Interacts (tyrosine phosphorylated) with CRK, GRB2 and GRB7. {ECO:0000250, ECO:0000269|PubMed:10733900, ECO:0000269|PubMed:11095946, ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11882663, ECO:0000269|PubMed:14644164, ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:2173144, ECO:0000269|PubMed:2536956, ECO:0000269|PubMed:2544881, ECO:0000269|PubMed:7535778, ECO:0000269|PubMed:7679113, ECO:0000269|PubMed:8940081, ECO:0000269|PubMed:8943348}.; SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus/HHV-5 envelope glycoprotein B/gB. Interacts also with the trimeric complex gH-gL-gO. Trimer-PDGFRA interaction has an inhibitory effect on PDGFRA signaling (PubMed:33626330). {ECO:0000269|PubMed:20660204, ECO:0000269|PubMed:28403202, ECO:0000269|PubMed:33626330}.
Post-translational modification
PTM: N-glycosylated.; PTM: Ubiquitinated, leading to its internalization and degradation. {ECO:0000305|PubMed:21596750}.; 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-731 and Tyr-742 is important for interaction with PIK3R1. Phosphorylation at Tyr-720 and Tyr-754 is important for interaction with PTPN11. Phosphorylation at Tyr-762 is important for interaction with CRK. Phosphorylation at Tyr-572 and Tyr-574 is important for interaction with SRC and SRC family members. Phosphorylation at Tyr-988 and Tyr-1018 is important for interaction with PLCG1. {ECO:0000269|PubMed:10733900, ECO:0000269|PubMed:10734113, ECO:0000269|PubMed:11095946, ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:7535778, ECO:0000269|PubMed:8943348}.
Target Relevance information above includes information from UniProt accession : P16234
The UniProt Consortium


ELISA with Biotinylated Human PDGF R alpha/PDGFRA Protein
Immobilized Anti-PDGF R alpha Antibody, hFc Tag T at 2µg/ml (100µl/Well) on the plate. Dose response curve for Biotinylated Human PDGF R alpha, His Tag with the EC50 of 0.16µg/ml determined by ELISA.
HPLC of Biotinylated Human PDGF R alpha/PDGFRA Protein
The purity of Biotinylated Human PDGF R alpha is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Biotinylated Human PDGF R alpha/PDGFRA Protein
Biotinylated Human PDGF R alpha on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.


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.



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