Human PDGF-D Antibody Summary
Ser250-Arg370
Accession # Q9GZP0.1
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Cell Proliferation Induced by PDGF‑DD and Neutralization by Human PDGF‑D Antibody. Recombinant Human PDGF-DD (Catalog # 1159-SB) stimulates proliferation in the NR6R-3T3 mouse fibroblast cell line in a dose-dependent manner (orange line). Proliferation elicited by Recombinant Human PDGF-DD (0.75 ug/mL) is neutralized (green line) by increasing concentrations of Mouse Anti-Human PDGF-D Monoclonal Antibody (Catalog # MAB1159). The ND50 is typically 1.5-7.5 µg/mL.
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Detection of PDGF-D by Immunocytochemistry/ Immunofluorescence Antioxidant effect of enriched proteins in SHED-CM. (A) Representative immunofluorescence images of MitoSOX analysis with nuclear DAPI staining of human acinar cell line 24 h after irradiation. Scale bar: 100 μm. (B) Quantitative analysis of the fluorescence intensities of MitoSOX analysis. The average fluorescence intensities were significantly higher in the irradiated cells treated with SHED-CM together with anti-PDGF-D antibodies or anti-HGF antibodies than those treated with SHED-CM alone. The antioxidant effect of SHED-CM was most strongly inhibited after treatment with four neutralizing antibodies together. Comparisons between groups were analyzed using an ANOVA with Tukey's multiple comparison test. Data are represented as mean ± SD (**p < 0.01, ***p < 0.001). CM, conditioned medium; HGF, hepatocyte growth factor; Fibro, fibroblast; PDGF, platelet-derived growth factor; SHED, stem cells from human exfoliated deciduous teeth. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/36792628), licensed under a CC-BY license. Not internally tested by R&D Systems.
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Detection of PDGF-D by Immunocytochemistry/ Immunofluorescence Antioxidant effect of enriched proteins in SHED-CM. (A) Representative immunofluorescence images of MitoSOX analysis with nuclear DAPI staining of human acinar cell line 24 h after irradiation. Scale bar: 100 μm. (B) Quantitative analysis of the fluorescence intensities of MitoSOX analysis. The average fluorescence intensities were significantly higher in the irradiated cells treated with SHED-CM together with anti-PDGF-D antibodies or anti-HGF antibodies than those treated with SHED-CM alone. The antioxidant effect of SHED-CM was most strongly inhibited after treatment with four neutralizing antibodies together. Comparisons between groups were analyzed using an ANOVA with Tukey's multiple comparison test. Data are represented as mean ± SD (**p < 0.01, ***p < 0.001). CM, conditioned medium; HGF, hepatocyte growth factor; Fibro, fibroblast; PDGF, platelet-derived growth factor; SHED, stem cells from human exfoliated deciduous teeth. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/36792628), licensed under a CC-BY license. Not internally tested by R&D Systems.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: PDGF-D
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.
- Xu, L. et al. (2005) Canc. Res. 65:5711.
Product Datasheets
Citations for Human PDGF-D Antibody
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.
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Phenotypic plasticity in normal breast derived epithelial cells.
Authors: Sauder C, Koziel J, Choi M, Fox M, Grimes B, Badve S, Blosser R, Radovich M, Lam C, Vaughan M, Herbert B, Clare S
BMC Cell Biol, 2014-06-10;15(0):20.
Species: Human
Sample Types: Whole Cells
Applications: ICC -
Therapeutic benefits of factors derived from stem cells from human exfoliated deciduous teeth for radiation-induced mouse xerostomia
Authors: F Kano, N Hashimoto, Y Liu, L Xia, T Nishihara, W Oki, K Kawarabaya, N Mizusawa, K Aota, T Sakai, M Azuma, H Hibi, T Iwasaki, T Iwamoto, N Horimai, A Yamamoto
Scientific Reports, 2023-02-15;13(1):2706.
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