protein

Human PDGFR alpha Recombinant

MBS553024

0.02 mg

220 USD

Recombinant Protein

Human PDGFR alpha Recombinant

PDGFR alpha

Human CD140a Recombinant (PDGF Receptor alpha) ; cd-140 PDGFRA; CD140A; MGC74795; PDGFR2; Rhe-PDGFRA PDGF Receptor alpha; pdgf-r

platelet-derived growth factor receptor alpha; Platelet-derived growth factor receptor alpha; 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

CD140a

PDGF-R

PDGFRA; PDGFR2; RHEPDGFRA; PDGF-R-alpha; PDGFR-alpha; PDGFR-2

PGFRA_HUMAN

HEk293 Cells

1089

>95%, as determined by SDS-PAGE and HPLC

Recombinant CD140a is supplied as a 0.2 um filtered PBS solution, pH7.2.

Recombinant CD140a, as supplied, can be stored in working aliquots at 2 degree - 8 degree C for one month, or at -20 degree C to -70 degree C for twelve months. Avoid repeated freeze/thaw cycles.

Biological Activity: The Activity was measured by the ability to bind human PDGFC-Fc in functional ELISA. Domain: Ig-like C2. Host Note: Optimized DNA sequence encoding Human extracellular domain of human PDGF-R alpha including a C-terminal 6His tag was expressed in HEK293 cells.

Endotoxin: Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than 0.1 ng/ug (1EU/ug). Molecular Weight Note: Recombinant PDGFRa is a monomer protein consisting of 510 amino acid residue subunits, due to glycosylation migrates as an approximately 90-100 kDa protein on SDS-PAGE.

Receptors CD

The PDGFR/PDGF system includes two receptors (PDGFRA and PDGFRB) and four ligands (PDGFA, PDGFB, PDGFC, and PDGFD. Ligand binding induces receptor dimerization, enabling autophosphorylation of specific tyrosine residues and subsequent recruitment of a variety of signal transduction molecules. PDGFR regulates normal cellular growth and differentiation, and expression of activated PDGFR promotes oncogenic transformation, suggesting that activating mutations or gene rearrangements could play a role in human tumorigenesis. Numerous in vitro and in vivo studies showed that inhibition of PDGFRA signaling disrupts cancer cell survival in the subset of GISTs with activating PDGFRA mutations.

pdgfralpha signaling in the primary cilium regulates nhe1-dependent fibroblast migration via coordinated differential activity of mek1/2-erk1/2-p90rsk and akt signaling pathways . J. Cell Sci., Dec 2012; 10.1242/jcs.116426. functional expression of sk channels in murine detrusor pdgfralpha+ cells . J. Physiol., Dec 2012; 10.1113/jphysiol.2012.241505. pdgfralpha and cd51 mark human nestin+ sphere-forming mesenchymal stem cells capable of robust hematopoietic stem cell expansion . Blood (ASH Annual Meeting Abstracts), Nov 2012; 120: 505. candidate human primary mesenchymal stem/progenitor cells are highly enriched in linneg/cd45neg/cd271pos/pdgfralphaneg bone marrow cells . Blood (ASH Annual Meeting Abstracts), Nov 2012; 120: 3460. stromal platelet-derived growth factor receptor alpha (pdgfralpha) provides a therapeutic target independent of tumor cell pdgfralpha expression in lung cancer xenografts . Mol. Cancer Ther., Nov 2012; 11: 2473 - 2482.

5453870

NP_006197.1

NM_006206.4

P16234

ATF-2 Transcription Factor Network Pathway (138006); Calcium Signaling Pathway (83050); Calcium Signaling Pathway (459); Cytokine-cytokine Receptor Interaction Pathway (83051); Cytokine-cytokine Receptor Interaction Pathway (460); Down-stream Signal Transduction Pathway (106385); Endocytosis Pathway (102279); Endocytosis Pathway (102181); Focal Adhesion Pathway (198795); Focal Adhesion Pathway (83067)

This gene encodes a cell surface tyrosine kinase receptor for members of the platelet-derived growth factor family. These growth factors are mitogens for cells of mesenchymal origin. The identity of the growth factor bound to a receptor monomer determines whether the functional receptor is a homodimer or a heterodimer, composed of both platelet-derived growth factor receptor alpha and beta polypeptides. Studies suggest that this gene plays a role in organ development, wound healing, and tumor progression. Mutations in this gene have been associated with idiopathic hypereosinophilic syndrome, somatic and familial gastrointestinal stromal tumors, and a variety of other cancers. [provided by RefSeq, Mar 2012]

PDGFRA: a receptor tyrosine kinase of the PDGFR family that binds members of the platelet-derived growth factor family. The identity of the growth factor bound determines whether the functional receptor is a homodimer or a heterodimer, composed of both PDGFR-alpha and -beta. Ligand binding induces receptor dimerization and autophosphorylation. Particularly important for kidney development since mice heterozygous for the receptor exhibit defective kidney phenotypes. Chromosomal rearrangments activate PDGFRalpha by fusion to BCR, causing atypical chronic myelogenous leukemia (CML), and to FIP1L1, causing idiopathic hypereosinophilic syndrome. Activating point mutations cause a minority of gastrointestinal stromal tumors (GIST). Promoter polymorphisms linked to neural tube defects including spina bifida, verified by mouse mutant model. Inhibitors: Gleevec, Sutent. OMIM: Two alternatively-spliced isoforms have been described. Protein type: Membrane protein, integral; Protein kinase, tyrosine (receptor); Protein kinase, TK; Kinase, protein; EC 2.7.10.1; Oncoprotein; TK group; PDGFR family. Chromosomal Location of Human Ortholog: 4q12. Cellular Component: microvillus; membrane; integral to plasma membrane; cytoplasm; plasma membrane; nucleus; intrinsic to plasma membrane; external side of plasma membrane. Molecular Function: vascular endothelial growth factor receptor activity; protein binding; protein homodimerization activity; platelet-derived growth factor binding; platelet-derived growth factor receptor binding; platelet-derived growth factor alpha-receptor activity; transmembrane receptor protein tyrosine kinase activity; ATP binding. Biological Process: estrogen metabolic process; extracellular matrix organization and biogenesis; peptidyl-tyrosine phosphorylation; regulation of chemotaxis; nerve growth factor receptor signaling pathway; wound healing; viral reproduction; protein amino acid autophosphorylation; cardiac myofibril assembly; platelet-derived growth factor receptor signaling pathway; palate development; elevation of cytosolic calcium ion concentration; positive regulation of fibroblast proliferation; Leydig cell differentiation; embryonic digestive tract morphogenesis; luteinization; positive regulation of cell proliferation; male genitalia development; epidermal growth factor receptor signaling pathway; fibroblast growth factor receptor signaling pathway; phosphoinositide-mediated signaling; adrenal gland development; in utero embryonic development; positive regulation of phosphoinositide 3-kinase activity; embryonic cranial skeleton morphogenesis; odontogenesis of dentine-containing teeth; embryonic skeletal morphogenesis; positive regulation of phosphoinositide 3-kinase cascade; cell activation; innate immune response; hemopoietic progenitor cell differentiation; positive regulation of DNA replication; positive regulation of cell migration; lung development. Disease: Gastrointestinal Stromal Tumor; Hypereosinophilic Syndrome, Idiopathic

0.02 mg

220 USD

0.1 mg

595

0.5 mg

2220