Embryos (200 per condition) in early cellularization were hand-selected under a dissecting microscope and rapidly snap-frozen in liquid nitrogen. Frozen embryos were homogenized on ice in lysis buffer (150 μL 0.05 M Tris pH 8.0, 0.15 M KCl, 0.05M EDTA, 0.5% NP-40, 1X protease inhibitor cocktail (Pierce Protease Inhibitor Mini Tablets, EDTA-free, Thermo Scientific)). After spinning to remove yolk and debris, protein concentrations were determined using a BCA Protein Assay (Thermo Scientific). Equal amounts of protein were loaded per well and separated on hand-cast 12% SDS-PAGE gels. Proteins were transferred to 0.2 μm nitrocellulose (Bio-Rad, Hercules, CA) and probed with 1:50 mouse anti-β-actin (sc-47778, Santa Cruz Biotechnology, Dallas, TX), 1:5000 rabbit anti-Dm-Cofilin, or 1:5000 rabbit anti-Pi-Cofilin (sc-12912-R, Santa Cruz Biotechnology), followed by 1:5000 goat anti-mouse HRP or 1:10,000 goat anti-rabbit HRP secondary antibodies (Jackson Immuno Research, West Grove, PA).
Rabbit anti dm cofilin
Manufactured by Santa Cruz Biotechnology
Rabbit anti-Dm-Cofilin is a primary antibody product that specifically binds to the Cofilin protein from Drosophila melanogaster. Cofilin is an actin-binding protein that plays a crucial role in the regulation of actin dynamics within cells.
Automatically generated - may contain errors
Lab products found in correlation
Bca protein assay, by Thermo Fisher Scientific (4 mentions)
Mouse anti β actin sc 47778, by Santa Cruz Biotechnology (2 mentions)
Rabbit anti pi cofilin sc 12912 r, by Santa Cruz Biotechnology (2 mentions)
Goat anti rabbit hrp secondary antibody, by Jackson ImmunoResearch (2 mentions)
Goat anti mouse hrp, by Jackson ImmunoResearch (2 mentions)
Pierce protease inhibitor mini tablet, by Thermo Fisher Scientific (2 mentions)
0.2 μm nitrocellulose, by Bio-Rad (2 mentions)
2 protocols using rabbit anti dm cofilin
1
Protein Extraction and Analysis in Early Cellularizing Drosophila Embryos
2
Protein Extraction and Analysis in Early Cellularizing Drosophila Embryos
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Embryos (200 per condition) in early cellularization were hand-selected under a dissecting microscope and rapidly snap-frozen in liquid nitrogen. Frozen embryos were homogenized on ice in lysis buffer (150 μL 0.05 M Tris pH 8.0, 0.15 M KCl, 0.05M EDTA, 0.5% NP-40, 1X protease inhibitor cocktail (Pierce Protease Inhibitor Mini Tablets, EDTA-free, Thermo Scientific)). After spinning to remove yolk and debris, protein concentrations were determined using a BCA Protein Assay (Thermo Scientific). Equal amounts of protein were loaded per well and separated on hand-cast 12% SDS-PAGE gels. Proteins were transferred to 0.2 μm nitrocellulose (Bio-Rad, Hercules, CA) and probed with 1:50 mouse anti-β-actin (sc-47778, Santa Cruz Biotechnology, Dallas, TX), 1:5000 rabbit anti-Dm-Cofilin, or 1:5000 rabbit anti-Pi-Cofilin (sc-12912-R, Santa Cruz Biotechnology), followed by 1:5000 goat anti-mouse HRP or 1:10,000 goat anti-rabbit HRP secondary antibodies (Jackson Immuno Research, West Grove, PA).
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