Recombinant Human PDGF-CC (carrier-free)

Pricing & Availability
Regulatory Status
RUO
Other Names
Platelet-derived growth factor CC, PDGFCC, PDGF-CC
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Product Citations
publications
Human_PDGF-CC_RECOM_CF_061517
Human PDGF-CC induces proliferation of NIH3T3 mouse embryonic fibroblast cells in a dose dependent manner with ED50 of 0.05 - 0.2 µg/mL.
  • Human_PDGF-CC_RECOM_CF_061517
    Human PDGF-CC induces proliferation of NIH3T3 mouse embryonic fibroblast cells in a dose dependent manner with ED50 of 0.05 - 0.2 µg/mL.
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766702 5 µg £61
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766704 20 µg £150
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Description

Platelet-derived growth factors (PDGFs) are homo- or heterodimers of four polypeptides, known as A, B, C and D chains.  PDGF was initially discovered as a major mitogenic factor present in serum but absent from plasma.  Five PDGF isoforms (AA, BB, AB, CC and DD) have been identified.  The dimeric isoforms of PDGFs are differentially expressed in various cell types and their effects are mediated through distinct dimeric receptors made up of two structurally similar protein-tyrosine kinase receptor subunits (αα-, αβ-, or ββ-PDGFR).  PDGF-AA, AB, and BB dimers are processed intracellularly and secreted as active dimers that readily activate PDGF receptors.  PDGF-CC and DD are secreted as full-length, latent dimers, and the proteolytic removal of a CUB domain is required for the growth factor domain of PDGF-CC or DD to activate the PDGF receptors.  PDGFs are potent mitogens for connective tissue cells, including dermal fibroblasts, glial cells, arterial smooth muscle cells and some epithelial and endothelial cells.  PDGFs usually act primarily in paracrine manner and may be engaged in autocrine loops in tumors.  In addition to its activity as a mitogen, PDGF is chemotactic for fibroblasts, smooth muscle cells, neutrophils and mononuclear cells.

Product Details
Technical Data Sheet (pdf)

Product Details

Source
Human PDG-CC, amino acids Val235-Gly345 (Accession # NP_057289) was expressed in E. Coli.
Molecular Mass
The 112 amino acid recombinant proteins has predicted molecular mass of approximately 12.6 kD. The predicted N-terminal amino acid is Met.
Purity
>98%, as determined by SDS-PAGE gel and HPLC analysis.
Formulation
Lyophilized from 0.2 µm filtered protein solution in 5 mM sodium citrate.
Endotoxin Level
Less than 1 EU per µg protein as determined by the LAL method.
Storage & Handling
Unopened vial can be stored at -20°C or -70°C for one year. For maximum results, quick spin vial prior to opening. Reconstitute in water to a concentration of 0.1-0.5 mg/ml. Reconstituted samples can be kept at 4°C for one week and six months at -20°C or -70°C. Do not vortex. It is recommended to further dilute in a buffer containing a carrier protein such as 0.1% BSA and store working aliquots at -20°C or -70°C. Avoid repeated freeze/thaw cycles.
Activity
ED50 = 0.05 – 0.2 µg/mL as measured by the ability of protein to induce proliferation of NIH3T3 mouse embryonic fibroblast cells. Deep Blue Cell Vialibity Kit was used to quantitate cell proliferation.
Application

Bioassay

Antigen Details

Structure
Homodimer
Distribution

Platelets, Monocytes, Macrophages, Mast Cells

Function
Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin.
Interaction
Platelets, Fibroblast, Endothelial cells, Epithelial cells, Muscle cells, Neurons, Astrocytes, Oligodendrocytes, Neutrophils
Ligand/Receptor
PDGFR-αα, PDGFR-αβ
Bioactivity
Measured by its ability to induce proliferation of NIH3T3 cells.
Biology Area
Angiogenesis, Cell Biology, Immunology, Neuroscience, Neuroscience Cell Markers, Stem Cells
Molecular Family
Cytokines/Chemokines, Growth Factors
Antigen References

1. Heldin CH and Westermark B. 1999. Physiol. Rev. 79:1283.
2. Fredriksson L, et al. 2004. Cytokine Growth Factor Rev. 15:197.
3. Hu JG, et al. 2012. J. Mol. Neurosci. 46:644.
4. Schneider L, et al. 2010. Cell Physiol. Biochem. 25:279.
5. Karlsson C and Paulsson Y. 1994. J. Cell Physiol. 158:256.
6. Shure D, et al. 1992. Biochem. Biophys. Res. Commun. 186:1510.
7. Carlin SM, et al. 2003. Am. J. Physiol. Lung Cell Mol. Physiol. 284:L1020
8. Ustach CV, et al. 2005 Mol. Cell Biol. 25:6279-6288.
9. Jones AV and Cross NC. 2004. Cell Mol. Life Sci. 61:2912-23.
10. Andrae J, et al. 2008. Genes Dev. 22:1276-312.

Gene ID
56034 View all products for this Gene ID
UniProt
View information about PDGF-CC on UniProt.org

Related FAQs

Why choose BioLegend recombinant proteins?

     • Each lot of product is quality-tested for bioactivity as indicated on the data sheet.
     • Greater than 95% Purity or higher, tested on every lot of product.
     • 100% Satisfaction Guarantee for quality performance, stability, and consistency.
     • Ready-to-use liquid format saves time and reduces challenges associated with reconstitution.
     • Bulk and customization available. Contact us.
     • Learn more about our Recombinant Proteins.

How does the activity of your recombinant proteins compare to competitors?

We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!

What is the specific activity or ED50 of my recombinant protein?

The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.

Have your recombinants been tested for stability?

Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.

Does specific activity of a recombinant protein vary between lots?

Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.

How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?

Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)

Go To Top Version: 0    Revision Date: 06/16/2017

For Research Use Only. Not for diagnostic or therapeutic use.

 

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