Recombinant Drosophila Decapentaplegic (Dpp) Protein, CF


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Recombinant Drosophila Decapentaplegic (Dpp) Protein, CF Summary

Details of Functionality
Measured by its ability to induce Mad phosphorylation in S2 Drosophila cells transfected with Mad. Approximately 3 µg/mL of recombinant Drosophila DPP and higher can effectively induce Mad phosphorylation. Measured by its ability to induce alkaline phosphatase production by ATDC5 mouse chondrogenic cells. Nakamura, K. et al. (1999) Exp. Cell Res. 250:351. The ED50 for this effect is 0.5‑2 µg/mL.
E. coli-derived drosophila Decapentaplegic/DPP protein
Asp457-Arg588 (Gln473His) & (Pro474Ala), with an N-terminal Met
Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.


  • Bioactivity
  • Bioactivity2
Theoretical MW
14.8 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.
Read Publications using
159-DP/CF in the following applications:

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 4 mM HCl.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Drosophila Decapentaplegic (Dpp) Protein, CF

  • Decapentaplegic
  • DPP


Decapentaplegic (Dpp) is one of at least five TGF-beta superfamily ligands identified in the Drosophila genome. Dpp, a functional orthologue of mammalian BMP-2 and BMP-4, is a morphogen and plays an essential role in Drosophila development. Dpp regulates embryonic dorsal-ventral polarity and is required for gut morphogenesis and outgrowth and patterning of imaginal disks. Similar to other TGF-beta family ligands, Dpp is synthesized as a large proprotein which is proteolytically processed at the dibasic cleavage site to release the carboxy-terminal domain. Biologically active Dpp is a disulfide-linked homodimer of the carboxy-terminal 132 amino acid residues that contains the characteristic conserved cysteine residues involved in the formation of the cysteine knot and the interchain disulfide bond. Cellular responses to Dpp have been shown to be mediated by the ligand-induced formation of heteromeric complexes of the Drosophila type I, Thick Veins (Tkv), and type II, Punt, serine/threonine kinases. The activated receptor complex induces the phosphorylation of the prototypical Smad, Mad, and subsequent translocation of the Mad-Medea complex to the nucleus where they regulate the transcription of target genes. Secreted extracellular Dpp antagonists, including the short-gastrulation (Sog) and twisted gastrulation (TSG), which bind Dpp and regulate its availability, have been identified.

  1. Raftery, L.A. and D.J. Sutherland (1999) Dev. Biol. 210:251.
  2. Ruberte, E. et al. (1995) Cell 80:890.

Publications for Decapentaplegic/DPP (159-DP/CF)(8)

We have publications tested in 2 confirmed species: Drosophila, Insect - Gryllus.

We have publications tested in 4 applications: Binding Assay, Bioassay, ELISA Developmet, In vivo.

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Binding Assay
ELISA Developmet
In vivo
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Insect - Gryllus
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Showing Publications 1 - 8 of 8.
Publications using 159-DP/CF Applications Species
SJ Neal, D Dolezal, N Jusi?, F Pignoni Drosophila ML-DmD17-c3 cells respond robustly to Dpp and exhibit complex transcriptional feedback on BMP signaling components BMC Dev. Biol., 2019;19(1):1. 2019 [PMID: 30669963] (Bioassay, Drosophila) Bioassay Drosophila
Mapping signaling pathway cross-talk in Drosophila cells Proc Natl Acad Sci USA, 2016;0(0):. 2016 [PMID: 27528688] (Bioassay, Drosophila) Bioassay Drosophila
Winstanley J, Sawala A, Baldock C, Ashe H Synthetic enzyme-substrate tethering obviates the Tolloid-ECM interaction during Drosophila BMP gradient formation. Elife, 2015;4(0):. 2015 [PMID: 25642644] (Bioassay, Drosophila) Bioassay Drosophila
Zeng Z, de Gorter D, Kowalski M, ten Dijke P, Shimmi O Ter94/VCP is a novel component involved in BMP signaling. PLoS ONE, 2014;9(12):e114475. 2014 [PMID: 25469707] (Bioassay, Drosophila) Bioassay Drosophila
Donoughe S, Nakamura T, Ewen-Campen B, Green D, Henderson L, Extavour C BMP signaling is required for the generation of primordial germ cells in an insect. Proc Natl Acad Sci U S A, 2014;111(11):4133-8. 2014 [PMID: 24591634] (In vivo, Insect - Gryllus) In vivo Insect - Gryllus
Chen J, Honeyager SM, Schleede J Crossveinless d is a vitellogenin-like lipoprotein that binds BMPs and HSPGs, and is required for normal BMP signaling in the Drosophila wing. Development, 2012;139(12):2170-6. 2012 [PMID: 22573617] (Bioassay, Drosophila) Bioassay Drosophila
Wang Z, Flax LA, Kemp MM, Linhardt RJ, Baron MJ Host and pathogen glycosaminoglycan-binding proteins modulate antimicrobial peptide responses in Drosophila melanogaster. Infect. Immun., 2011;79(2):606-16. 2011 [PMID: 21078848] (ELISA Developmet, Drosophila) ELISA Developmet Drosophila
Serpe M, Umulis D, Ralston A, Chen J, Olson DJ, Avanesov A, Othmer H, O'Connor MB, Blair SS The BMP-binding protein Crossveinless 2 is a short-range, concentration-dependent, biphasic modulator of BMP signaling in Drosophila. Dev. Cell, 2008;14(6):940-53. 2008 [PMID: 18539121] (Binding Assay, Drosophila) Binding Assay Drosophila

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