Recombinant Human PDGF-DD Protein

• Reactivity: Hu
• Applications: Bioactivity

Recombinant Human PDGF-DD Protein 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 3.00‑36.0 ng/mL.
• Source: Mouse myeloma cell line, NS0-derived human PDGF-DD protein
  Ser250-Arg370
• Accession #: Q9GZP0.1
• 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

• 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

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 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).

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.

Publications for PDGF-DD (1159-SB)(19)

Publications using 1159-SB

• Mohanakrishnan, V;Sivaraj, KK;Jeong, HW;Bovay, E;Dharmalingam, B;Bixel, MG;Dinh, VV;Petkova, M;Paredes Ugarte, I;Kuo, YT;Gurusamy, M;Raftrey, B;Chu, NTL;Das, S;Rios Coronado, PE;Stehling, M;Sävendahl, L;Chagin, AS;Mäkinen, T;Red-Horse, K;Adams, RH; Specialized post-arterial capillaries facilitate adult bone remodelling Nature cell biology 2024-11-11 [PMID: 39528700] (Bioassay, Human)
• Wong, KG;Cheng, YF;Wu, VH;Kiseleva, AA;Li, J;Poleshko, A;Smith, CL;Epstein, JA; Growth factor-induced activation of MSK2 leads to phosphorylation of H3K9me2S10 and corresponding changes in gene expression Science advances 2024-03-15 [PMID: 38478612] (Bioassay, Human)
• HJ Kim, P Cheng, S Travisano, C Weldy, JP Monteiro, R Kundu, T Nguyen, D Sharma, H Shi, Y Lin, B Liu, S Haldar, S Jackson, T Quertermou Molecular mechanisms of coronary artery disease risk at the PDGFD locus Nature Communications, 2023-02-15;14(1):847. 2023-02-15 [PMID: 36792607] (Bioassay, Human)
• T Akiyama, T Yasuda, T Uchihara, N Yasuda-Yos, BJY Tan, A Yonemura, T Semba, J Yamasaki, Y Komohara, K Ohnishi, F Wei, L Fu, J Zhang, F Kitamura, K Yamashita, K Eto, S Iwagami, H Tsukamoto, T Umemoto, M Masuda, O Nagano, Y Satou, H Saya, P Tan, H Baba, T Ishimoto Stromal reprogramming through dual PDGFRalpha/beta blockade boosts the efficacy of anti-PD-1 immunotherapy in fibrotic tumors Cancer Research, 2023-03-02;0(0):. 2023-03-02 [PMID: 36543251] (Bioassay, Human)
• T Pham, AJ Najy, HC Kim E3 ligase HUWE1 promotes PDGF D-mediated osteoblastic differentiation of mesenchymal stem cells by effecting polyubiquitination of beta-PDGFR The Journal of Biological Chemistry, 2022-04-25;0(0):101981. 2022-04-25 [PMID: 35472332] (Bioassay, Human)
• Z Li, S Yu, Y Liu, X Hu, Y Li, Z Xiao, Y Chen, D Tian, X Xu, L Cheng, M Zheng, J Jing SU16f inhibits fibrotic scar formation and facilitates axon regeneration and locomotor function recovery after spinal cord injury by blocking the PDGFRbeta pathway Journal of Neuroinflammation, 2022-04-16;19(1):95. 2022-04-16 [PMID: 35429978] (In Vivo, Mouse)
• JO Kim, SE Baek, EY Jeon, JM Choi, EJ Jang, CD Kim PDGFR-beta signaling mediates HMGB1 release in mechanically stressed vascular smooth muscle cells PLoS ONE, 2022-03-16;17(3):e0265191. 2022-03-16 [PMID: 35294955] (Bioassay, Rat)
• Y Yamamoto, A Mukai, T Ikushima, Y Urata, S Kinoshita, J Hamuro, M Ueno, C Sotozono Pluripotent epigenetic regulator OBP-801 maintains filtering blebs in glaucoma filtration surgery model Scientific Reports, 2020-12-01;10(1):20936. 2020-12-01 [PMID: 33262357] (Cell Culture, Human)
• 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, 2017-11-27;7(1):16439. 2017-11-27 [PMID: 29180757] (Surface Plasmon Resonance, Human)
• Integrative functional genomics identifies regulatory mechanisms at coronary artery disease loci Nat Commun, 2016-07-08;7(0):12092. 2016-07-08 [PMID: 27386823] (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, 2015-08-10;112(34):E4717-25. 2015-08-10 [PMID: 26261320] (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, 2015-03-25;520(7547):368-72. 2015-03-25 [PMID: 25807485] (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, 2013-08-01;288(38):27273-86. 2013-08-01 [PMID: 23908351] (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, 2012-07-26;487(7408):505-9. 2012-07-26 [PMID: 22763448] (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., 2010-07-29;24(12):4711-21. 2010-07-29 [PMID: 20671107] (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, 2009-01-06;15(1):21-34. 2009-01-06 [PMID: 19111878] (Western Blot)
• 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., 2008-12-01;58(12):3765-75. 2008-12-01 [PMID: 19035474] (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, 2008-05-22;202(2):415-23. 2008-05-22 [PMID: 18573494] (Bioassay, Human)
• McCabe KL, Bronner-Fraser M Essential role for PDGF signaling in ophthalmic trigeminal placode induction. Development, 2008-04-16;135(10):1863-74. 2008-04-16 [PMID: 18417621] (In Vivo, Chicken)

Bioinformatics

• Gene Symbol: PDGFD
• Uniprot:
  • Q9GZP0.1()