Recombinant Drosophila Decapentaplegic (Dpp) Protein

• Reactivity: Dr
• Applications: Bioactivity

Recombinant Drosophila Decapentaplegic (Dpp) Protein 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.
• Source: E. coli-derived drosophila Decapentaplegic/DPP protein
  Asp457-Arg588 (Gln473His) & (Pro474Ala), with an N-terminal Met
• Accession #: NP_722813
• N-terminal Sequence: Met
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >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.

Applications/Dilutions

• Dilutions:
  • 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.

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 under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile 4 mM HCl 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 Drosophila Decapentaplegic (Dpp) Protein

• Decapentaplegic
• DPP

Background

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)(9)

Publications using 159-DP

• S Liu, GH Baeg, Y Yang, FG Goh, H Bao, EJ Wagner, X Yang, Y Cai The Integrator complex desensitizes cellular response to TGF-beta/BMP signaling Cell Reports, 2023-01-14;42(1):112007. 2023-01-14 [PMID: 36641752] (Bioassay, Drosophila melanogaster)
• 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., 2019-01-22;19(1):1. 2019-01-22 [PMID: 30669963] (Bioassay, Drosophila)
• Mapping signaling pathway cross-talk in Drosophila cells Proc Natl Acad Sci USA, 2016-08-15;0(0):. 2016-08-15 [PMID: 27528688] (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, 2015-02-02;4(0):. 2015-02-02 [PMID: 25642644] (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, 2014-12-03;9(12):e114475. 2014-12-03 [PMID: 25469707] (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, 2014-03-03;111(11):4133-8. 2014-03-03 [PMID: 24591634] (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, 2012-05-09;139(12):2170-6. 2012-05-09 [PMID: 22573617] (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., 2010-11-15;79(2):606-16. 2010-11-15 [PMID: 21078848] (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, 2008-06-01;14(6):940-53. 2008-06-01 [PMID: 18539121] (Binding Assay, Drosophila)

Bioinformatics

• Uniprot:
  • NP_722813()