For Western blots, the protein samples were separated by SDS-PAGE on 12% gels then transferred to nitrocellulose membranes. After blocking the nonspecific binding sites with 3% BSA in TBST (20 mM Tris pH 7.4, 0.1% Tween 20, 150 mM NaCl), the membranes were incubated with rabbit anti-phospho-p44/42 (1:1000 dilution; Cell Signaling, Danvers, MA, USA), or rabbit anti-p44/42 (1:1000 dilution; Cell Signaling) antibodies. The proteins were detected with horseradish peroxidase-conjugated secondary antibodies using the West Save Gold western blot detection kit (Ab Frontier, Seoul, Korea). The immunoreactive bands were visualized using a Chemiluminescence imaging system (Syngene, Cambridge, United Kingdom).
West save gold western blot detection kit
Manufactured by AbFrontier
The West Save Gold western blot detection kit is a laboratory equipment product that is used for the detection and visualization of proteins separated by western blot analysis. This kit provides the necessary reagents and components to perform the western blot detection process.
Automatically generated - may contain errors
Lab products found in correlation
Microchemi, by DNR Bio-Imaging Systems (2 mentions)
Chemiluminescence imaging system, by Syngene (1 mentions)
Rabbit anti phospho p44 42, by Cell Signaling Technology (1 mentions)
Rabbit anti p44 42, by Cell Signaling Technology (1 mentions)
Anti glyceraldehyde 3 phosphate dehydrogenase gapdh, by Cell Signaling Technology (1 mentions)
Anti trpv1, by Santa Cruz Biotechnology (1 mentions)
Anti α tubulin, by Merck Group (1 mentions)
Anti ha tag, by Cell Signaling Technology (1 mentions)
Anti β actin, by Merck Group (1 mentions)
Mouse anti β actin, by Merck Group (1 mentions)
3 protocols using west save gold western blot detection kit
1
Western Blot Protein Analysis
2
Western Blot Protocol for Protein Detection
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For western blots, protein samples were separated using 10% sodium dodecyl
sulphate-polyacrylamide gel electrophoresis and transferred to nitrocellulose
membranes. After blocking with 5% nonfat dry milk in TBST (20 mM Tris, pH 7.4,
0.1% Tween 20, 150 mM NaCl), membranes were incubated with anti-HA-Tag (Cell
Signaling, Danvers, MA, USA), anti-TRPV1 (Santa Cruz, Dallas, TX, USA),
anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (Cell Signaling),
anti-β-actin (Sigma-Aldrich), or anti-α-tubulin (Sigma-Aldrich) antibodies.
Proteins were detected with horseradish peroxidase-conjugated secondary
antibodies using the West Save Gold western blot detection kit (Ab Frontier,
Seoul, Korea). Signals were visualized by MicroChemi (DNR Bio-imaging Systems,
Jerusalem, Israel).
sulphate-polyacrylamide gel electrophoresis and transferred to nitrocellulose
membranes. After blocking with 5% nonfat dry milk in TBST (20 mM Tris, pH 7.4,
0.1% Tween 20, 150 mM NaCl), membranes were incubated with anti-HA-Tag (Cell
Signaling, Danvers, MA, USA), anti-TRPV1 (Santa Cruz, Dallas, TX, USA),
anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (Cell Signaling),
anti-β-actin (Sigma-Aldrich), or anti-α-tubulin (Sigma-Aldrich) antibodies.
Proteins were detected with horseradish peroxidase-conjugated secondary
antibodies using the West Save Gold western blot detection kit (Ab Frontier,
Seoul, Korea). Signals were visualized by MicroChemi (DNR Bio-imaging Systems,
Jerusalem, Israel).
3
Histamine Receptor H1 Western Blot
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For western blots, protein samples were separated using 10% SDS-PAGE and transferred to nitrocellulose membranes. After blocking with 5% nonfat dry milk in TBST (20 mM Tris, pH 7.4, 0.1% Tween 20, 150 mM NaCl), membranes were incubated with rabbit anti-histamine receptor H1 (1:500, Santa Cruz), or mouse anti-β-actin (1:5000, Sigma-Aldrich) antibodies. Proteins were detected with horseradish peroxidase conjugated secondary antibodies using West Save Gold western blot detection kit (Ab Frontier, Seoul, Korea). Signal was visualized by MicroChemi (DNR Bio-imaging Systems, Jerusalem, Israel).
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