Recombinant Human PDGF-CC Protein

• Reactivity: Hu
• Applications: Bioactivity

Recombinant Human PDGF-CC Protein 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 #: NP_057289
• 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

• Dilutions:
  • Bioactivity
• 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.

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 with BSA as a carrier protein.
• 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 containing at least 0.1% human or bovine serum albumin.

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

• 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.

Publications for PDGF-CC (1687-CC)(14)

Publications using 1687-CC

• T Akiyama, T Yasuda, T Uchihara, N Yasuda-Yos, BJY Tan, A Yonemura, T Semba, J Yamasaki, Y Komohara, K Ohnishi, F Wei, L Fu, J Zhang, F Kitamura, K Yamashita, K Eto, S Iwagami, H Tsukamoto, T Umemoto, M Masuda, O Nagano, Y Satou, H Saya, P Tan, H Baba, T Ishimoto Stromal reprogramming through dual PDGFRalpha/beta blockade boosts the efficacy of anti-PD-1 immunotherapy in fibrotic tumors Cancer Research, 2023-03-02;0(0):. 2023-03-02 [PMID: 36543251] (Bioassay, Human)
• Li Q, Ming Y, Jia H, Wang G Poricoic acid A suppresses TGF-beta1-induced renal fibrosis and proliferation via the PDGF-C, Smad3 and MAPK pathways. Exp Ther Med, 2021-01-27;21(4):289. 2021-01-27 [PMID: 33717232] (Bioassay, Rat)
• Y Yamamoto, A Mukai, T Ikushima, Y Urata, S Kinoshita, J Hamuro, M Ueno, C Sotozono Pluripotent epigenetic regulator OBP-801 maintains filtering blebs in glaucoma filtration surgery model Scientific Reports, 2020-12-01;10(1):20936. 2020-12-01 [PMID: 33262357] (Cell Culture, Human)
• R Lopez-Bell, S Puig, PJ Huang, CR Tsai, HN Turner, MJ Galko, HB Gutstein Growth factor signaling regulates mechanical nociception in flies and vertebrates J. Neurosci., 2019-05-28;0(0):. 2019-05-28 [PMID: 31138657] (Bioassay, In Vivo, Rat)
• F Mahjour, V Dambal, N Shrestha, V Singh, V Noonan, A Kantarci, PC Trackman Mechanism for oral tumor cell lysyl oxidase like-2 in cancer development: synergy with PDGF-AB Oncogenesis, 2019-05-13;8(5):34. 2019-05-13 [PMID: 31086173] (Bioassay, Human)
• 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, 2017-11-27;7(1):16439. 2017-11-27 [PMID: 29180757] (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, 2017-03-02;7(0):43736. 2017-03-02 [PMID: 28252047] (Bioassay, Human)
• Endothelial PDGF-CC regulates angiogenesis-dependent thermogenesis in beige fat Nat Commun, 2016-08-05;7(0):12152. 2016-08-05 [PMID: 27492130] (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, 2014-03-25;9(3):e92925. 2014-03-25 [PMID: 24667490] (Bioassay, Human)
• Son D, Na Y, Hwang E, Seok S Platelet-derived growth factor-C (PDGF-C) induces anti-apoptotic effects on macrophages through Akt and Bad phosphorylation. J Biol Chem, 2014-01-13;289(9):6225-35. 2014-01-13 [PMID: 24421315] (Bioassay, Human)
• Fenny Wiradjaja, Denny L. Cottle, Lynelle Jones, Ian Smyth Regulation of PDGFC signalling and extracellular matrix composition by FREM1 in mice Disease Models & Mechanisms 2013-09-19 [PMID: 24046351] (Bioassay, Mouse, Transgenic Mouse)
• Ball SG, Bayley C, Shuttleworth CA, Kielty CM Neuropilin-1 regulates platelet-derived growth factor receptor signalling in mesenchymal stem cells. Biochem. J., 2010-03-15;427(1):29-40. 2010-03-15 [PMID: 20102335] (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, 2009-01-06;15(1):21-34. 2009-01-06 [PMID: 19111878] (Western Blot)
• 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, 2008-05-22;202(2):415-23. 2008-05-22 [PMID: 18573494] (Bioassay, Human)

Bioinformatics

• Gene Symbol: PDGFC
• Uniprot:
  • NP_057289()