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
>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
Dilutions
Bioactivity
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 in the following applications:
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 with BSA as a carrier protein.
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 HCI containing at least 0.1% human or bovine serum albumin.
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
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).
Reigstad, L.J. et al. (2005) FEBS J. 272:5723.
Fredriksson, L. et al. (2004) Cytokine Growth Factor Rev. 15:197.
LaRochelle, W.J. et al. (2001) Nat. Cell Biol. 3:517.
Bergsten, E. et al. (2001) Nat. Cell Biol. 3:512.
Uutela, M. et al. (2004) Blood 104:3198.
Ustach, C.V. and H-R.C. Kim (2005) Mol. Cell. Biol. 25:6279.
Ustach, C.V. et al. (2004) Canc. Res. 64:1722.
Zhuo, Y. et al. (2003) Biochem. Biophys. Res. Commun. 308:126.
Changsirikulchai, S. et al. (2002) Kid. Int. 62:2043.
Ray, S. et al. (2005) J. Biol. Chem. 280:8494.
Hudkins, K.L. et al. (2004) J. Am. Soc. Nephrol. 15:286.
Lokker, N.A. et al. (2002) Canc. Res. 62:3729.
Taneda, S. et al. (2003) J. Am. Soc. Nephrol. 14:2544.
LaRochelle, W.J. et al. (2002) Canc. Res. 62:2468.
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