• Purity

  >97%, by SDS-PAGE under reducing conditions and visualized by silver stain

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured in a cell proliferation assay using NR6R?3T3 mouse fibroblast cells. Raines, E.W.     et al. (1985) Methods Enzymol.     109:749. The ED    ₅₀ for this effect is 70-350 ng/mL.

• Source

  E. coli-derived Val235-Gly345, with an N-terminal Met and a 6-His tag

• Accession #

• N-terminal Sequence    
  Analysis

  Met

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  13.4 kDa (monomer)

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: PDGF-CC

The platelet-derived growth factor (PDGF) family consists of proteins derived from four genes (PDGF-A, -B, -C, and -D) that form four disulfide-linked homodimers (PDGF-AA, -BB, -CC, and -DD) and one heterodimer (PDGF-AB) (1). These proteins regulate diverse cellular functions by binding to and inducing the homo- or hetero-dimerization of two receptor tyrosine kinases (PDGF R alpha  and R beta ). Within the PDGF family, PDGF-C and PDGF-D constitute a subgroup that shares similar structural organization (2, 3). Both proteins are secreted as inactive homodimeric latent growth factors. Each monomer has two distinct protein domains: an N-terminal CUB domain; and a C-terminal PDGF/VEGF homology domain that shares 27 - 35% sequence identity with the corresponding regions of other PDGF family members. An 80 - 90 amino acid residue hinge region connects the two domains. Sequential removal of the CUB domains in the homodimeric latent growth factor by extracellular proteolytic cleavage at the hinge region is required to release the bioactive PDGF/VEGF homology domain (1). Twelve cysteine residues are found within the PDGF/VEGF homology domain of PDGF-C, including the characteristic eight invariant cysteine residues involved in inter- and intra-chains disulfide-bonds needed for the formation of the cysteine-knot structure. Bioactive PDGF-CC binds with high-affinity to PDGF R alpha  but not PDGF R beta  and activates PDGF R alpha homodimerization (1). PDGF-CC has also been shown to activate PDGF R alpha beta heterodimers (1). PDGF-CC is expressed in multiple embryonic and adult cell types and tissues. During embryonic development, PDGF-CC is involved in ductal morphogenesis (4). PDGF-CC is a potent angiogenic factor that stimulates vessel growth in the mouse cornea pocket assay and in the CAM assay (5). It stimulates coronary artery smooth muscle cell proliferation and may play an important role in cardiovascular development and function (6). PDGF-CC is also expressed in many tumors and tumor cell lines and has a causative role in tumorigenesis (7). Mature human and mouse PDGF-C share 93.7% amino acid sequence identity.

• References:

1. Li, X. and U. Eriksson (2003) Cytokine & Growth Factor Rev. 14:91.

2. LaRochells, W.J. et al. (2001) Nature Cell Biol. 3:517.

3. Li, X. et al. (2000) Nature Cell Biol. 2:302.

4. Aase, K. et al. (2002) Mech. Dev. 110:187.

5. Cao, R.H. et al. (2002) FASEB J. 16:1575.

6. Gilbertson, D. et al. (2001) J. Biol. Chem. 276:27406.

7. Zwerner, J.P. and W.A. May (2001) Oncogene 20:626.  

• Long Name:

  Platelet-derived Growth Factor CC

• Entrez Gene IDs:

  56034 (Human); 54635 (Mouse)

• Alternate Names:

  PDGFCC; PDGF-CC