Recombinant Drosophila Decapentaplegic (Dpp) Protein

Carrier Free

Catalog # Availability Size / Price Qty
159-DP-020/CF

With Carrier

Catalog # Availability Size / Price Qty
159-DP-020
R&D Systems Recombinant Proteins and Enzymes
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Citations (9)
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Recombinant Drosophila Decapentaplegic (Dpp) Protein Summary

Product Specifications

Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
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 #
N-terminal Sequence
Analysis
Met
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
14.8 kDa (monomer)

Product Datasheets

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159-DP (with carrier)

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159-DP/CF (carrier free)

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

159-DP

Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile 4 mM HCl containing at least 0.1% human or bovine serum albumin.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

159-DP/CF

Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
Reconstitution Reconstitute at 100 μg/mL in sterile 4 mM HCl.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
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Background: 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.

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

Citations for Recombinant Drosophila Decapentaplegic (Dpp) Protein

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.

9 Citations: Showing 1 - 9
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  1. The Integrator complex desensitizes cellular response to TGF-beta/BMP signaling
    Authors: S Liu, GH Baeg, Y Yang, FG Goh, H Bao, EJ Wagner, X Yang, Y Cai
    Cell Reports, 2023-01-14;42(1):112007.
    Species: Drosophila melanogaster
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Drosophila ML-DmD17-c3 cells respond robustly to Dpp and exhibit complex transcriptional feedback on BMP signaling components
    Authors: SJ Neal, D Dolezal, N Jusi?, F Pignoni
    BMC Dev. Biol., 2019-01-22;19(1):1.
    Species: Drosophila
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Mapping signaling pathway cross-talk in Drosophila cells
    Proc Natl Acad Sci USA, 2016-08-15;0(0):.
    Species: Drosophila
    Sample Types: Whole Cells
    Applications: Bioassay
  4. Synthetic enzyme-substrate tethering obviates the Tolloid-ECM interaction during Drosophila BMP gradient formation.
    Authors: Winstanley J, Sawala A, Baldock C, Ashe H
    Elife, 2015-02-02;4(0):.
    Species: Drosophila
    Sample Types: Protein
    Applications: Bioassay
  5. Ter94/VCP is a novel component involved in BMP signaling.
    Authors: Zeng Z, de Gorter D, Kowalski M, ten Dijke P, Shimmi O
    PLoS ONE, 2014-12-03;9(12):e114475.
    Species: Drosophila
    Sample Types: Whole Cells
    Applications: Bioassay
  6. BMP signaling is required for the generation of primordial germ cells in an insect.
    Authors: Donoughe S, Nakamura T, Ewen-Campen B, Green D, Henderson L, Extavour C
    Proc Natl Acad Sci U S A, 2014-03-03;111(11):4133-8.
    Species: Insect - Gryllus
    Sample Types: Whole Embryo
    Applications: In Vivo
  7. Crossveinless d is a vitellogenin-like lipoprotein that binds BMPs and HSPGs, and is required for normal BMP signaling in the Drosophila wing.
    Authors: Chen J, Honeyager SM, Schleede J
    Development, 2012-05-09;139(12):2170-6.
    Species: Drosophila
    Sample Types: Whole Cells
    Applications: Bioassay
  8. Host and pathogen glycosaminoglycan-binding proteins modulate antimicrobial peptide responses in Drosophila melanogaster.
    Authors: Wang Z, Flax LA, Kemp MM, Linhardt RJ, Baron MJ
    Infect. Immun., 2010-11-15;79(2):606-16.
    Species: Drosophila
    Sample Types:
    Applications: ELISA Developmet
  9. The BMP-binding protein Crossveinless 2 is a short-range, concentration-dependent, biphasic modulator of BMP signaling in Drosophila.
    Authors: Serpe M, Umulis D, Ralston A, Chen J, Olson DJ, Avanesov A, Othmer H, O'Connor MB, Blair SS
    Dev. Cell, 2008-06-01;14(6):940-53.
    Species: Drosophila
    Sample Types: Recombinant Protein
    Applications: Binding Assay

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