货号 | AF159-SP |
别名 | DPP |
应用 | Western Blot(0.1 µg/mL) |
目标/特异性 | DetectsDrosophila Decapentaplegic/DPP in direct ELISAs and Western blots. In direct ELISAs and Western blots, less than 1% cross‑reactivity with recombinant human (rh) TGF-beta 1, rhTGF-beta 2, rhTGF-beta 3, and recombinant amphibian TGF‑ beta 5 is observed. |
使用方法 | Western Blot: 0.1 µg/mL |
来源 | Reconstitute at 0.2 mg/mL in sterile PBS. |
产品组分 |
供应商 | R&D Systems |
应用文献 | |
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. The BMP-binding protein Crossveinless 2 is a short-range, concentration-dependent, biphasic modulator of BMP signaling in Drosophila. | |
纯化方式 | Antigen Affinity-purified from egg yolks |
免疫原 | E. coli-derived recombinant DrosophilaDecapentaplegic/DPP Asp457-Arg588 (Gln473His, Pro474Ala) Accession # P07713 |
内毒素水平 | <0.10 EU per 1 μg of the antibody by the LAL method. |
生物活性 | Drosophila |
标记 | Unconjugated |
溶解方法 | Reconstitute at 0.2 mg/mL in sterile PBS. |
背景 | 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 Drosophilatype 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. |
运输条件 | Blue Ice |
存放说明 | 4℃ |
参考文献 |
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