Recombinant Human PDGF-DD Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human PDGF-DD 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 15‑75 ng/mL in a fluorometric assay using the redox sensitive dye, Resazurin (Catalog # AR002) and 2-5 ng/mL when measured by 3H-thymidine incorporation.
Source
Mouse myeloma cell line, NS0-derived human PDGF-DD protein
Ser250-Arg370
Accession #
N-terminal Sequence
Ser250
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
PDGFD
Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
14 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.
SDS-PAGE
19 kDa, reducing conditions
Publications
Read Publications using
1159-SB/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 visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
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-DD Protein, CF

  • PDGFDD
  • PDGF-DD

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 human PDGF-DD cDNA encodes a 370 amino acid (aa) precursor that includes a 23 aa signal sequence, one CUB domain, and one PDGF/VEGF domain (3, 4). The PDGF/VEGF domain shares 27 - 35% aa sequence identity with the corresponding regions of other PDGF family members. Human PDGF-DD shares 87% aa sequence identity with mouse and rat PDGF-DD. PDGF-DD is secreted as a100 kDa latent homodimer which is activated by proteolysis to release a 35 kDa bioactive protein containing the PDGF/VEGF homology 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 overexpressed 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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1159-SB/CF
Species: Hu
Applications: Bioactivity

Publications for PDGF-DD (1159-SB/CF)(11)

We have publications tested in 4 confirmed species: Human, Mouse, Chicken, N/A.

We have publications tested in 4 applications: Bioassay, In Vivo, Surface Plasmon Resonance, Western Blot.


Filter By Application
Bioassay
(7)
In Vivo
(1)
Surface Plasmon Resonance
(2)
Western Blot
(1)
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Human
(8)
Mouse
(1)
Chicken
(1)
N/A
(1)
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Showing Publications 1 - 10 of 11. Show All 11 Publications.
Publications using 1159-SB/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
Integrative functional genomics identifies regulatory mechanisms at coronary artery disease loci Nat Commun, 2016;7(0):12092. 2016 [PMID: 27386823] (Bioassay, Human) Bioassay Human
Heim E, Marston J, Federman R, Edwards A, Karabadzhak A, Petti L, Engelman D, DiMaio D Biologically active LIL proteins built with minimal chemical diversity. Proc Natl Acad Sci U S A, 2015;112(34):E4717-25. 2015 [PMID: 26261320] (Bioassay, Human) Bioassay Human
Obenauf A, Zou Y, Ji A, Vanharanta S, Shu W, Shi H, Kong X, Bosenberg M, Wiesner T, Rosen N, Lo R, Massague J Therapy-induced tumour secretomes promote resistance and tumour progression. Nature, 2015;520(7547):368-72. 2015 [PMID: 25807485] (Bioassay, Human) Bioassay Human
Petti L, Talbert-Slagle K, Hochstrasser M, DiMaio D A single amino acid substitution converts a transmembrane protein activator of the platelet-derived growth factor beta receptor into an inhibitor. J Biol Chem, 2013;288(38):27273-86. 2013 [PMID: 23908351] (Bioassay, Human) Bioassay Human
Wilson TR, Fridlyand J, Yan Y, Penuel E, Burton L, Chan E, Peng J, Lin E, Wang Y, Sosman J, Ribas A, Li J, Moffat J, Sutherlin DP, Koeppen H, Merchant M, Neve R, Settleman J Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors. Nature, 2012;487(7408):505-9. 2012 [PMID: 22763448] (Bioassay, Human) Bioassay Human
Martino MM, Hubbell JA The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain. FASEB J., 2010;24(12):4711-21. 2010 [PMID: 20671107] (Surface Plasmon Resonance, Human) Surface Plasmon Resonance 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] (Western Blot, N/A) Western Blot N/A
Rice JW, Veal JM, Fadden RP, Barabasz AF, Partridge JM, Barta TE, Dubois LG, Huang KH, Mabbett SR, Silinski MA, Steed PM, Hall SE Small molecule inhibitors of Hsp90 potently affect inflammatory disease pathways and exhibit activity in models of rheumatoid arthritis. Arthritis Rheum., 2008;58(12):3765-75. 2008 [PMID: 19035474] (Bioassay, Mouse) Bioassay Mouse
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
Show All 11 Publications.

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Bioinformatics

Gene Symbol PDGFD
Uniprot