Home / PDGF-CC / Recombinant Human PDGF-CC Protein

Recombinant Human PDGF-CC Protein

Catalog #: 1687-CC
13 Citations Datasheet / COA / SDS

Carrier Free

Catalog # Availability Size / Price Qty
1687-CC-025/CF

With Carrier

Catalog # Availability Size / Price Qty
1687-CC-025
R&D Systems Recombinant Proteins and Enzymes
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Product Details
Citations (13)
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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human PDGF-CC Protein Summary

Product Specifications

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 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
Analysis
Met
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
13.4 kDa (monomer)

Product Datasheets

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1687-CC (with carrier)

Product Datasheet
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1687-CC/CF (carrier free)

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COA
SDS

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.

1687-CC

Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile 4 mM HCl containing at least 0.1% human or bovine serum albumin.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

1687-CC/CF

Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
Reconstitution Reconstitute at 100 μg/mL in sterile 4 mM HCl.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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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

Citations for Recombinant Human PDGF-CC Protein

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

13 Citations: Showing 1 - 10
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  1. Stromal reprogramming through dual PDGFRalpha/beta blockade boosts the efficacy of anti-PD-1 immunotherapy in fibrotic tumors
    Authors: 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
    Cancer Research, 2023-03-02;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Poricoic acid A suppresses TGF-beta1-induced renal fibrosis and proliferation via the PDGF-C, Smad3 and MAPK pathways.
    Authors: Li Q, Ming Y, Jia H, Wang G
    Exp Ther Med, 2021-01-27;21(4):289.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Pluripotent epigenetic regulator OBP-801 maintains filtering blebs in glaucoma filtration surgery model
    Authors: Y Yamamoto, A Mukai, T Ikushima, Y Urata, S Kinoshita, J Hamuro, M Ueno, C Sotozono
    Scientific Reports, 2020-12-01;10(1):20936.
    Species: Human
    Sample Types: Whole Cells
    Applications: Cell Culture
  4. Growth factor signaling regulates mechanical nociception in flies and vertebrates
    Authors: R Lopez-Bell, S Puig, PJ Huang, CR Tsai, HN Turner, MJ Galko, HB Gutstein
    J. Neurosci., 2019-05-28;0(0):.
    Species: Rat
    Sample Types: In Vivo
    Applications: Bioassay, In Vivo
  5. Mechanism for oral tumor cell lysyl oxidase like-2 in cancer development: synergy with PDGF-AB
    Authors: F Mahjour, V Dambal, N Shrestha, V Singh, V Noonan, A Kantarci, PC Trackman
    Oncogenesis, 2019-05-13;8(5):34.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Discovery of High-Affinity PDGF-VEGFR Interactions: Redefining RTK Dynamics
    Authors: SB Mamer, S Chen, JC Weddell, A Palasz, A Wittenkell, M Kumar, PI Imoukhuede
    Sci Rep, 2017-11-27;7(1):16439.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Surface Plasmon Resonance
  7. Inhibition of Proliferation and Epithelial Mesenchymal Transition in Retinal Pigment Epithelial Cells by Heavy Chain-Hyaluronan/Pentraxin 3
    Authors: H He, AE Kuriyan, CW Su, M Mahabole, Y Zhang, YT Zhu, HW Flynn, JM Parel, SC Tseng
    Sci Rep, 2017-03-02;7(0):43736.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  8. Endothelial PDGF-CC regulates angiogenesis-dependent thermogenesis in beige fat
    Nat Commun, 2016-08-05;7(0):12152.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  9. Activation of platelet-derived growth factor receptor alpha contributes to liver fibrosis.
    Authors: Hayes B, Riehle K, Shimizu-Albergine M, Bauer R, Hudkins K, Johansson F, Yeh M, Mahoney W, Yeung R, Campbell J
    PLoS ONE, 2014-03-25;9(3):e92925.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  10. Platelet-derived growth factor-C (PDGF-C) induces anti-apoptotic effects on macrophages through Akt and Bad phosphorylation.
    Authors: Son D, Na Y, Hwang E, Seok S
    J Biol Chem, 2014-01-13;289(9):6225-35.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  11. Neuropilin-1 regulates platelet-derived growth factor receptor signalling in mesenchymal stem cells.
    Authors: Ball SG, Bayley C, Shuttleworth CA, Kielty CM
    Biochem. J., 2010-03-15;427(1):29-40.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  12. PDGF-C mediates the angiogenic and tumorigenic properties of fibroblasts associated with tumors refractory to anti-VEGF treatment.
    Authors: Crawford Y, Kasman I, Yu L, Zhong C, Wu X, Modrusan Z, Kaminker J, Ferrara N
    Cancer Cell, 2009-01-06;15(1):21-34.
    Applications: Western Blot
  13. Effects of PDGF-C and PDGF-D on monocyte migration and MMP-2 and MMP-9 expression.
    Authors: Wagsater D, Zhu C, Bjorck HM, Eriksson P
    Atherosclerosis, 2008-05-22;202(2):415-23.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay

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