Recombinant Human PDGF-CC Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human PDGF-CC Protein, CF Summary

Details of Functionality
Measured in a cell proliferation assay using NR6R‑3T3 mouse fibroblast cells. Raines, E.W. et al. (1985) Methods Enzymol. 109:749. The ED50 for this effect is 70-350 ng/mL.
Source
E. coli-derived human PDGF-CC protein
Val235-Gly345, with an N-terminal Met and 6-His tag
Accession #
N-terminal Sequence
Met
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
PDGFC
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
13.4 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.
Publications
Read Publications using
1687-CC/CF 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 Acetonitrile and TFA.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 4 mM HCl.

Notes

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

Alternate Names for Recombinant Human PDGF-CC Protein, CF

  • PDGFCC
  • PDGF-CC

Background

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.

  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.

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1687-CC/CF
Species: Hu
Applications: Bioactivity

Publications for PDGF-CC (1687-CC/CF)(7)

We have publications tested in 2 confirmed species: Human, N/A.

We have publications tested in 3 applications: Bioassay, Surface Plasmon Resonance, WB Ctrl.


Filter By Application
Bioassay
(5)
Surface Plasmon Resonance
(1)
WB Ctrl
(1)
All Applications
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Human
(6)
N/A
(1)
All Species
Showing Publications 1 - 7 of 7.
Publications using 1687-CC/CF Applications Species
SB Mamer, S Chen, JC Weddell, A Palasz, A Wittenkell, M Kumar, PI Imoukhuede Discovery of High-Affinity PDGF-VEGFR Interactions: Redefining RTK Dynamics Sci Rep, 2017;7(1):16439. 2017 [PMID: 29180757] (Surface Plasmon Resonance, Human) Surface Plasmon Resonance Human
H He, AE Kuriyan, CW Su, M Mahabole, Y Zhang, YT Zhu, HW Flynn, JM Parel, SC Tseng Inhibition of Proliferation and Epithelial Mesenchymal Transition in Retinal Pigment Epithelial Cells by Heavy Chain-Hyaluronan/Pentraxin 3 Sci Rep, 2017;7(0):43736. 2017 [PMID: 28252047] (Bioassay, Human) Bioassay Human
Endothelial PDGF-CC regulates angiogenesis-dependent thermogenesis in beige fat Nat Commun, 2016;7(0):12152. 2016 [PMID: 27492130] (Bioassay, Human) Bioassay Human
Hayes B, Riehle K, Shimizu-Albergine M, Bauer R, Hudkins K, Johansson F, Yeh M, Mahoney W, Yeung R, Campbell J Activation of platelet-derived growth factor receptor alpha contributes to liver fibrosis. PLoS ONE, 2014;9(3):e92925. 2014 [PMID: 24667490] (Bioassay, Human) Bioassay Human
Ball SG, Bayley C, Shuttleworth CA, Kielty CM Neuropilin-1 regulates platelet-derived growth factor receptor signalling in mesenchymal stem cells. Biochem. J., 2010;427(1):29-40. 2010 [PMID: 20102335] (Bioassay, Human) Bioassay Human
Crawford Y, Kasman I, Yu L, Zhong C, Wu X, Modrusan Z, Kaminker J, Ferrara N PDGF-C mediates the angiogenic and tumorigenic properties of fibroblasts associated with tumors refractory to anti-VEGF treatment. Cancer Cell, 2009;15(1):21-34. 2009 [PMID: 19111878] (WB Ctrl, N/A) WB Ctrl N/A
Wagsater D, Zhu C, Bjorck HM, Eriksson P Effects of PDGF-C and PDGF-D on monocyte migration and MMP-2 and MMP-9 expression. Atherosclerosis, 2009;202(2):415-23. 2009 [PMID: 18573494] (Bioassay, Human) Bioassay Human

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Bioinformatics

Gene Symbol PDGFC
Uniprot