Recombinant Human PDGF R alpha Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human PDGF R alpha Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit the biological activity of PDGF-AB or PDGF-AA using NR6R‑3T3 mouse fibroblast cells. Raines, E.W. et al. (1985) Methods Enzymol. 109:749.

The ED50 for this effect is 0.2-1 μg/mL in the presence of 100 ng/mL recombinant human PDGF-AB.

Source
Mouse myeloma cell line, NS0-derived human PDGF R alpha protein
Human PDGF R alpha
(Met1 - Glu524)
Accession # P16234
IEGRMD Human IgG1
(Pro100 - Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Gln24
Protein/Peptide Type
Recombinant Proteins
Gene
PDGFRA
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
82.8 kDa (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
110-130 kDa, reducing conditions
Publications
Read Publications using
6765-PR in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human PDGF R alpha Fc Chimera Protein, CF

  • alpha-type platelet-derived growth factor receptor
  • CD140 antigen-like family member A
  • CD140a antigen
  • CD140a
  • EC 2.7.10
  • EC 2.7.10.1
  • MGC74795
  • PDGF R alpha
  • PDGFR alpha
  • PDGFR2
  • PDGFRA
  • PDGFRA/BCR fusion
  • PDGF-R-alpha
  • platelet-derived growth factor receptor, alpha polypeptide
  • rearranged-in-hypereosinophilia-platelet derived growth factor receptor alphafusion protein
  • RHEPDGFRA

Background

PDGF R alpha (platelet-derived growth factor receptor alpha) is a type I transmembrane glycoprotein in the class III subfamily of receptor tyrosine kinases (RTK) (1 ‑ 4). PDGF R alpha and PDGF R beta can form homo- or hetero-dimeric receptors when engaged by dimers of the PDGF family of growth factors, which include disulfide-linked homodimers of PDGF-A, B, C or D, or the heterodimer PDGF-AB that is mainly found in human platelets. While multiple in vitro ligand-receptor combinations have been identified, in vivo evidence indicates that PDGF R alpha primarily binds PDGF-AA and PDGF-CC, while PDGF R beta primarily binds PDGF-BB and probably PDGF-DD. Like all class III RTKs, the extracellular domain (ECD) of human PDGF R alpha (aa 24 ‑ 524) contains five immunoglobulin-like domains, while the intracellular region contains a split tyrosine kinase domain (aa 593 ‑ 954) (1 ‑ 4). Within the ECD, human PDGF R alpha shares 85%, 83%, 95%, 93%, and 88% aa sequence identity with mouse, rat, equine, canine and bovine PDGF R alpha respectively. PDGF R alpha autophosphorylates upon dimerization, activating signaling cascades in PI 3-kinase Ras‑MAP kinase, and PLC-gamma pathways (1, 2). Signaling is down‑regulated by SHP-2 phosphatase activity and by receptor endocytosis and lysosomal degradation. PDGF R alpha is expressed at low levels in most mesenchymal cells, but is strongly expressed in oligodendrocyte, lung, skin and intestinal progenitor cells and induced by inflammation or growth in culture (1 ‑ 4). During development, mesenchymal cells expressing PDGF R alpha respond to local gradients of epithelially produced PDGF-AA or PDGF-CC during formation of the cranial and cardiac neural crest, retina, gonads, lung alveoli, intestinal villi, skin, hair follicles, skeleton, teeth, palate, and interstitial kidney mesenchyme (1, 5). Deletion of PDGF R alpha in mice severely impairs mesenchymal derivatives in both embryo and extraembryonic tissues, and high or low PDGF R alpha signaling in humans may result in spina bifida or cleft palate‑type malformations. Postnatally, PDGF R alpha is implicated in gliomas and fibrotic disorders of lung, heart and skin (scleroderma) (6 ‑ 8).

  1. Andrae, J. et al. (2008) Genes Dev. 22:1276.
  2. Heldin, C-H. and B. Westermark (1999) Physiol. Rev. 79:1283.
  3. Claesson-Welsh, L. et al. (1989) Proc. Natl. Acad. Sci. USA 86:4917.
  4. Matsui, T. et al. (1989) Science 243:800.
  5. Klinghoffer, R.A. et al. (2002) Dev. Cell 2:103.
  6. Martinho, O. (2009) Br. J. Cancer 101:973.
  7. Olson, L.E. and P. Soriano (2009) Dev. Cell 16:303.
  8. Baroni, S.S. et al. (2006) N. Engl. J. Med. 354:2667.

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Bioinformatics

Gene Symbol PDGFRA
Entrez
Uniprot