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Human PDGFRa / CD140a Protein

CD140A,PDGFR-2,PDGFR2,RHEPDGFRA

Catalog Number P10556-HCCH
Organism Species Human
Host Human Cells
Synonyms CD140A,PDGFR-2,PDGFR2,RHEPDGFRA
Molecular Weight The recombinant human PDGFRα consists of 507 amino acids and predicts a molecular mass of 56.8 kDa. By SDS-PAGE, the apparent molecular mass of rhPDGFRα is approximately 90-100 kDa due to the glycosylation.
predicted N Gln 24
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction The mature form of human PDGFRa (NP_006197.1) extracellular domain (Met 1-Glu 524) with five amino acids (DDDDK) at the C-terminus was expressed and purified.
Bio-activity Measured by its ability to bind mouse PDGF-C (P50458-M01H) in functional ELISA.
Research Area Immunology |Cytokines & Growth Factors |Growth Factor & Receptor |Platelet-Derived Growth Factor (PDGF) & Receptor |PDGF Receptor
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background PDGFRA, also known as CD140a, together with the structurally homolog protein PDGFRB (CD140b), are cell surface receptors for members of the platelet-derived growth factor family. They are members of the class III subfamily of receptor tyrosine kinase (RTKs) with the similar structure characteristics of five immunoglobulin-like domains in their extracellular region and a split kinase domain in their intracellular region. PDGFRA is expressed in oligodendrocyte progenitor cells and mesothelial cell, and binds all three ligand isoforms PDGF-AA, PDGF-BB and PDGF-AB with high affinity, whereas PDGFRB dose not bind PDGF-AA. PDGFRA plays an essential role in regulating proliferation, chemotaxis and migration of mesangial cells. Recent studies have indicated that PDGFRA acts as a critical mediator of signaling in testis organogenesis and Leydig cell differentiation, and in addition, particularly important for kidney development. Additionally, PDGFRA is involved in tumor angiogenesis and maintenance of the tumor microenvironment and has been implicated in development and metastasis of Hepatocellular carcinoma (HCC). PDGFRA may represent a potential therapeutic target in thymic tumours. PDGFRA gene amplification rather than gene mutation may be the underlying genetic mechanism driving PDGFRA overexpression in a portion of gliomas.
Reference
  • Oseini AM, et al. (2009) PDGFRalpha: a new therapeutic target in the treatment of hepatocellular carcinoma? Expert Opin Ther Targets. 13(4): 443-54.
  • Meister M, et al. (2009) Expression and mutational status of PDGFR in thymic tumours. Anticancer Res. 29(10): 4057-61.
  • Martinho O, et al. (2009) Expression, mutation and copy number analysis of platelet-derived growth factor receptor A (PDGFRA) and its ligand PDGFA in gliomas. Br J Cancer. 101(6): 973-82.