Proteins (75 µg) extracted from cyanobacterial strains were fractionated by performing SDS-PAGE 12%, and transferred to nitrocellulose membranes before being revealed with specific polyclonal antibodies. Immune complexes were detected with anti-rabbit peroxidase-conjugated secondary antibodies (Promega) and enhanced chemoluminescence reagents (Pierce). Anti-FlvB antibodies, developed against the FlvB protein of C. reinhardtii [18 (link)], were used at a 1: 1000 dilution. Anti-Rbcl antibodies (Agrisera) were used a 1: 5000 dilution.
Anti rabbit peroxidase conjugated secondary antibodies
Manufactured by Promega
Sourced in France
Anti-rabbit peroxidase-conjugated secondary antibodies are laboratory reagents designed to detect the presence of rabbit primary antibodies in various immunoassay techniques, such as Western blotting and immunohistochemistry. These secondary antibodies are conjugated with the enzyme peroxidase, which can be used to generate a colorimetric or chemiluminescent signal when exposed to an appropriate substrate, allowing the visualization and quantification of the target antigen.
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Lab products found in correlation
4 protocols using anti rabbit peroxidase conjugated secondary antibodies
1
Immunoblotting of Cyanobacterial Proteins
2
Western Blot Analysis of Signaling Proteins
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A western blot analysis was performed as described previously.11 (link) The antibodies that were used included anti-livin (SC-30161, 1:1000). Antibodies against ERK1/2 (sc-292838, 1:1000) and phospho-ERK1/2 (sc-23759-R, 1:2000) were purchased from Santa Cruz Biotechnology (USA). Antibodies against HER2 (ab8054, 1:500) were purchased from Abcam. Anti-phospho-AKT (SC-33437, 1:2000), anti-AKT (SC-1618, 1:1000), and mouse anti-fibronectin (SC18827, 1:1000) antibodies were purchased from Santa Cruz Biotechnology. Anti-vimentin (BS1776, 1:1000), anti-E-cadherin (BS1098, 1:1000), and anti-N-cadherin (BS222, 1:1000) antibodies were purchased from Bioworld Technology, and anti-rabbit peroxidase-conjugated secondary antibodies were purchased from Promega. An inhibitor of ERK1/2 (PD98059) was obtained from Santa Cruz Biotechnology (USA) and an inhibitor of AKT (LY294002) was obtained from Sigma-Aldrich (St. Louis, MO, USA).
3
SDS-PAGE Protein Fractionation and Immunoblotting
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Proteins were fractionated by performing SDS-PAGE (4–20%) stained with Coomassie blue (Euromedex, Souffelweyrshim, France). For immunoblot analysis, the proteins were transferred to nitrocellulose membranes before being revealed with anti-Histidine monoclonal antibodies (Qiagen). Immune complexes were detected with anti-rabbit peroxidase-conjugated secondary antibodies (Promega) and enhanced chemiluminescence reagents (Pierce, Illkich, France).
4
SDS-PAGE and Immunoblot Analysis
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Proteins were fractionated by performing SDS-PAGE (12% except where indicated) stained with Coomassie blue (Euromedex, Souffelweyrshim, France). For electrophoresis under non-reducing conditions, β-mercaptoethanol was omitted from the SDS-PAE gels, and the proteins were not heated before loading into the gel. For immunoblot analysis, the proteins were transferred to nitrocellulose membranes before being revealed with specific polyclonal antibodies. Immune complexes were detected with anti-rabbit peroxidase-conjugated secondary antibodies (Promega) and enhanced chemiluminescence reagents (Pierce, Illkich, France). Anti-HetR antibodies were developed by Covalab and used at a 1:1000 dilution.
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