Human PDGF-CC
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Cat-Nr. | 100-354 |
Size | 20 µg |
Price | 199 € |
Source | E. coli |
Formulation | lyophilized |
Purity Confirmation | > 98% by SDS-PAGE & HPLC analyses |
Length [aa] | 114 |
Molecular Weight | 25 kDa |
Endotoxin Levels | < 0.1 ng/µg of protein (<1EU/µg) |
Biological Activity | Determined by the dose-dependent stimulation of the proliferation of Balb/c 3T3 cells. The expected The ED50 for this effect is 15-20 ng/ml. |
Species Reactivity | Mouse, Human |
Synonyms | PDGF-CC |
Description | The platelet-derived growth factor (PDGF) family of heparin-binding growth factors consists of five known members, denoted PDGF-AA, PDGF-BB, PDGF-AB, PDGF-CC and PDGF-DD. The mature and active form of these proteins, an anti-parallel disulfide-linked dimer of two 12-14 kDa polypeptide chains, is obtained through proteolytic processing of biologically inactive precursor proteins, which contain an N-terminal CUB domain and a PDGF/VEGF homologous domain. The PDGFs interact with two related protein tyrosine kinase receptors, PDGFR-α and PDGFR-β, and are potent mitogens for a variety of cell types, including smooth muscle cells, connective tissue cells, bone and cartilage cells, and certain tumor cells. They play an important role in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubules epithelial cell development. Mature PDGFs are stored in platelet α-granules and are released upon platelet activation. PDGF-AA, -AB, -BB and –CC signal primarily through the PDGF-Rα receptor, whereas PDGF-DD interacts almost exclusively with the PDGF-Rβ receptor. Recombinant human PDGF-CC is a 25 kDa protein consisting of two identical disulfide-linked 114 amino-acid polypeptide chains. |
Protein Sequence | MVVDLNLLTE EVRLYSCTPR NFSVSIREEL KRTDTIFWPG CLLVKRCGGN CACCLHNCNE CQCVPSKVTK KYHEVLQLRP KTGVRGLHKS LTDVALEHHE ECDCVCRGST GG |
Uniprot ID | Q9NRA1 |
Protein RefSeq | NP_057289.1 |
mRNA RefSeq | NM_016205.2 |
Reference
- Platelet-derived growth factor-C promotes human melanoma aggressiveness through activation of neuropilin-1. F. Ruffini et al., Oncotarget. 2017 Sep 15; 8(40): 66833–66848.
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