Recombinant Human PDGF-DD Protein

Formulations:
Catalog # Availability Size / Price Qty
1159-SB-025
Product Details
Citations (11)
FAQs
Supplemental Products
Reviews

Recombinant Human PDGF-DD Protein Summary

Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.01 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 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
Analysis
Ser250
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
14 kDa (monomer)
SDS-PAGE
19 kDa, reducing conditions

Product Datasheets

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.

1159-SB

Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Reconstitution Reconstitute at 10 μg/mL in sterile 4 mM HCI 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.

1159-SB/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-DD

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).

References
  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.
Long Name
Platelet-derived Growth Factor DD
Entrez Gene IDs
80310 (Human)
Alternate Names
PDGFDD; PDGF-DD

Citations for Recombinant Human PDGF-DD 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.

11 Citations: Showing 1 - 10
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  1. 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;7(1):16439.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Surface Plasmon Resonance
  2. Integrative functional genomics identifies regulatory mechanisms at coronary artery disease loci
    Nat Commun, 2016;7(0):12092.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Biologically active LIL proteins built with minimal chemical diversity.
    Authors: Heim E, Marston J, Federman R, Edwards A, Karabadzhak A, Petti L, Engelman D, DiMaio D
    Proc Natl Acad Sci U S A, 2015;112(34):E4717-25.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  4. Therapy-induced tumour secretomes promote resistance and tumour progression.
    Authors: Obenauf A, Zou Y, Ji A, Vanharanta S, Shu W, Shi H, Kong X, Bosenberg M, Wiesner T, Rosen N, Lo R, Massague J
    Nature, 2015;520(7547):368-72.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. A single amino acid substitution converts a transmembrane protein activator of the platelet-derived growth factor beta receptor into an inhibitor.
    Authors: Petti L, Talbert-Slagle K, Hochstrasser M, DiMaio D
    J Biol Chem, 2013;288(38):27273-86.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors.
    Authors: 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
    Nature, 2012;487(7408):505-9.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  7. The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain.
    Authors: Martino MM, Hubbell JA
    FASEB J., 2010;24(12):4711-21.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Surface Plasmon Resonance
  8. 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, 2009;202(2):415-23.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  9. 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;15(1):21-34.
    Species: N/A
    Sample Types: N/A
    Applications: WB Ctrl
  10. Small molecule inhibitors of Hsp90 potently affect inflammatory disease pathways and exhibit activity in models of rheumatoid arthritis.
    Authors: Rice JW, Veal JM, Fadden RP, Barabasz AF, Partridge JM, Barta TE, Dubois LG, Huang KH, Mabbett SR, Silinski MA, Steed PM, Hall SE
    Arthritis Rheum., 2008;58(12):3765-75.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  11. Essential role for PDGF signaling in ophthalmic trigeminal placode induction.
    Authors: McCabe KL, Bronner-Fraser M
    Development, 2008;135(10):1863-74.
    Species: Chicken
    Sample Types: In Vivo
    Applications: In Vivo

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