Rhdll4

Manufactured by R&D Systems

Sourced in Germany, United Kingdom

RhDLL4 is a recombinant human Delta-like ligand 4 protein. Delta-like ligand 4 is a member of the Delta/Serrate/Lag-2 (DSL) family of Notch ligands. It functions as a ligand for the Notch receptor, which plays a crucial role in cell-cell communication and the regulation of various developmental processes.

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Lab products found in correlation

Nvp bhg712, by Novartis (1 mentions) Ruxolitinib, by InvivoGen (1 mentions) Il 10, by R&D Systems (1 mentions) Trypsin edta, by Thermo Fisher Scientific (1 mentions) Bovine serum albumin (bsa), by Merck Group (1 mentions)

3 protocols using rhdll4

HUVEC Signaling Pathway Modulation

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Human umbilical vein endothelial cells (HUVEC) were cultured in endothelial cell growth medium (ECGM) with supplement (Promocell, Heidelberg, Germany). To study the signalling pathways, cells were treated with different inhibitors and activators including a specific EphB4 kinase inhibitor NVP‐BHG712 (NVP) (kind gift from Novartis, Basel, Switzerland), ephrinB2‐Fc (B2fc; R&D System, Wiesbaden, Germany), recombinant human DLL4 (rhDLL4; R&D System) and γ‐secretase inhibitor DAPT (Sigma‐Aldrich, Munich, Germany) as indicated in the individual experiments.

You C., Zhao K., Dammann P., Keyvani K., Kreitschmann‐Andermahr I., Sure U, & Zhu Y. (2017). EphB4 forward signalling mediates angiogenesis caused by CCM3/PDCD10‐ablation. Journal of Cellular and Molecular Medicine, 21(9), 1848-1858.

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Macrophage Polarization Modulation

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Tissue culture plates were coated for 4 h with recombinant human DLL4 (rhDLL4) and DLL1 (rhDLL1) proteins purchased from R&D Systems (R&D Systems Europe Ltd., Abingdon, UK), diluted into PBS (5 μg/mL). Pharmacological inhibitors of γ-secretase (N-[N-(3,5-Difluorophenacetyl)-L-alanyl]-Sphenylglycine t butyl ester; DAPT, Sigma Aldrich, Lyon, France) and of JAK1/JAK2 (Ruxolitinib, Invivogen, Toulouse, France) were used at 0.5 μg/mL and 0.1 μg/mL, respectively. For the inhibition of γ-secretase, macrophages were incubated with DAPT (0.5 μg/mL; Sigma Aldrich) for the 48 h during or for 24 h following M1 or M2 polarization. Similarly, inhibition of JAK/STAT signaling pathway was achieved by adding Ruxolitinib (0.1 μg/mL; Invivogen) during the polarization step. Macrophage Colony Stimulating Factor (M-CSF), IL-4 and IL-10 were from R&D Systems.

Pagie S., Gérard N, & Charreau B. (2018). Notch signaling triggered via the ligand DLL4 impedes M2 macrophage differentiation and promotes their apoptosis. Cell Communication and Signaling : CCS, 16, 4.

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Induction of Endothelial Cell Quiescence

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Contact Inhibition Model of EC Quiescence ECs (p1 or p2) were seeded in 100% EGM2 at a density of 15,000 cells/cm 2 . During the progressive induction of EC-quiescence, the culture medium was gradually changed from 100% EGM2 to M199/EGM2 mix in ratio 1:1 (further referred to as growth medium). To generate the corresponding proliferative control, contact inhibited cells (day 6 QECs) were trypsinized (using Trypsin-EDTA (0.25%); Thermo Fisher Scientific) and cultured in growth medium for at least 36 hr to re-initiate proliferation. PECs, used as proliferating controls for contact-inhibited QECs are always reseeded QECs. Dll4 Stimulation Model of EC Quiescence Culture plates were coated overnight at 4 C on a plate shaker with 1 mg/mL recombinant human Delta like ligand4 (rhDll4, R&D Systems) with 0.1% gelatin. The control plates were coated with 0.1% gelatin supplemented with 0.02% BSA (Sigma-Aldrich), which was used as a carrier for Dll4. Prior to EC seeding, excessive coating solution was removed by aspiration and ECs were seeded at a density of 30,000 cells/cm 2 in growth medium. Experiments were performed 24 hr after seeding. PECs, used as proliferating controls for Dll4-induced QECs are always ECs grown in parallel on BSA coated plates.

Kalucka J., Bierhansl L., Conchinha N.V., Missiaen R., Elia I., Brüning U., Scheinok S., Treps L., Cantelmo A.R., Dubois C., de Zeeuw P., Goveia J., Zecchin A., Taverna F., Morales-Rodriguez F., Brajic A., Conradi L.C., Schoors S., Harjes U., Vriens K., Pilz G.A., Chen R., Cubbon R., Thienpont B., Cruys B., Wong B.W., Ghesquière B., Dewerchin M., De Bock K., Sagaert X., Jessberger S., Jones E.A.V., Gallez B., Lambrechts D., Mazzone M., Eelen G., Li X., Fendt S.M, & Carmeliet P. (2018). Quiescent Endothelial Cells Upregulate Fatty Acid β-Oxidation for Vasculoprotection via Redox Homeostasis. Cell metabolism, 28(6).

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