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Recombinant Mouse PDGF-D Protein, CF

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Recombinant Mouse PDGF-D (Catalog # 9738-SB)stimulates cell proliferation of the NR6R-3T3 mouse fibroblast cell line. TheED50 for this effect is 15-90 ng/mL.

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse PDGF-D 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 15-90 ng/mL
Source
Mouse myeloma cell line, NS0-derived mouse PDGF-D protein
Ser250-Arg370
Accession #
N-terminal Sequence
Ser250
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
14 kDa.
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.
SDS-PAGE
18-20 kDa, reducing conditions

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 HCl.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 250 μg/mL in 4 mM HCl.

Notes

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

Alternate Names for Recombinant Mouse PDGF-D Protein, CF

  • IEGFMSTP036
  • Iris-expressed growth factor
  • PDGFD
  • PDGF-D
  • platelet derived growth factor D
  • SCDGF-BMGC26867
  • SCDGFBplatelet-derived growth factor D
  • spinal cord derived growth factor B
  • Spinal cord-derived growth factor B
  • spinal cord-derived growth factor-B

Background

The platelet-derived growth factor (PDGF) family consists of four disulfide-linked homodimers and one heterodimer (PDGF-AB). These proteins regulate diverse cellular functions through interactions with PDGF R alpha and R beta (1, 2). Mature PDGF-DD associates with PDGF R beta and triggers signaling through PDGF R beta homodimers and PDGF R alpha / beta heterodimers (3-5). The mouse PDGF-DD cDNA encodes a 370 amino acid (aa) precursor that includes a 23 aa signal sequence, a 226 aa CUB domain, and a 121 aa PDGF/VEGF domain (3, 4). The PDGF/VEGF domain shares 27-35% aa sequence identity with the corresponding regions of other PDGF family members. Mouse PDGF-DD shares 91% and 98% aa sequence identity with human and rat PDGF-DD, respectively. PDGF-DD is secreted as a 100 kDa latent homodimer which is activated by proteolysis to release a 35 kDa bioactive protein containing the disulfide-linked dimer of PDGF/VEGF domain (3, 4, 6, 7). A splice variant of PDGF-DD has a 6 aa deletion near the N-terminus. A 72 aa deletion within the PDGF/VEGF domain generates an inactive protein in mouse but has not been detected in human (8). PDGF-DD is widely expressed in embryonic and adult tissues (3, 9, 10), and PDGF R beta is expressed in a generally complementary pattern (9, 11, 12). PDGF-DD functions as a growth factor for renal artery smooth muscle cells and lens epithelial cells, and as a macrophage chemoattractant (5, 9-11). PDGF-DD is over-expressed in and contributes to several disease states, including renal and hepatic fibrosis, mesangial proliferative glomerulopathy, pulmonary lymphoid infiltration, and many cancers (6, 11-15). PDGF-DD functions in both paracrine and autocrine manners (6, 7, 14).
  1. Reigstad, L.J. et al. (2005) FEBS J. 272:5723.
  2. Fredriksson, L. et al. (2004) Cytokine Growth Factor Rev. 15:197.
  3. LaRochelle, W.J. et al. (2001) Nat. Cell Biol. 3:517.
  4. Bergsten, E. et al. (2001) Nat. Cell Biol. 3:512.
  5. Uutela, M. et al. (2004) Blood 104:3198.
  6. Ustach, C.V. and H-R.C. Kim (2005) Mol. Cell. Biol. 25:6279.
  7. Ustach, C.V. et al. (2004) Canc. Res. 64:1722.
  8. Zhuo, Y. et al. (2003) Biochem. Biophys. Res. Commun. 308:126.
  9. Changsirikulchai, S. et al. (2002) Kid. Int. 62:2043.
  10. Ray, S. et al. (2005) J. Biol. Chem. 280:8494.
  11. Hudkins, K.L. et al. (2004) J. Am. Soc. Nephrol. 15:286.
  12. Lokker, N.A. et al. (2002) Canc. Res. 62:3729.
  13. Taneda, S. et al. (2003) J. Am. Soc. Nephrol. 14:2544.
  14. LaRochelle, W.J. et al. (2002) Canc. Res. 62:2468.
  15. Xu, L. et al. (2005) Canc. Res. 65:5711.

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