Proteins were isolated using glass bead lysis as described (Abrams et al, 2014). Protein samples were heated (65°C, 15 min) in SDS–PAGE sample-loading buffer, loaded into 10% bis-acrylamide/SDS gels and separated by electrophoresis. Separated protein samples were transferred to a polyvinylidene difluoride (PVDF) membrane, blocked in 5% nonfat dry milk and proteins detected using monoclonal anti-GFP (Roche), monoclonal anti-PGK (Invitrogen), and monoclonal anti-Ub (EMD Millipore) antibodies, followed by detection with HRP-conjugated secondary antibody (MilliporeSigma) with enhanced chemiluminescence reagent and direct photon emission imaging. Protein bands were quantitated using Image Studio Lite (LI-COR Biosciences).
Monoclonal anti ub
Manufactured by Merck Group
Monoclonal anti-Ub is a laboratory reagent that binds to ubiquitin, a small protein found in eukaryotic cells. It is used as a tool in biological research to study ubiquitin-related processes and protein dynamics.
Automatically generated - may contain errors
2 protocols using monoclonal anti ub
1
Quantitative Protein Immunoblotting Protocol
2
Protein Detection and Quantification
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Proteins were isolated using glass bead lysis as described (Abrams et al, 2014). Protein samples were heated (65°C, 15 min) in SDS-PAGE sample-loading buffer, loaded into 10% bis-acrylamide/SDS gels and separated by electrophoresis. Separated protein samples were transferred to a polyvinylidene difluoride (PVDF) membrane, blocked in 5% nonfat dry milk and proteins detected using monoclonal anti-GFP (Roche), monoclonal anti-PGK (Invitrogen), and monoclonal anti-Ub (EMD Millipore) antibodies, followed by detection with HRP-conjugated secondary antibody (MilliporeSigma) with enhanced chemiluminescence reagent and direct photon emission imaging. Protein bands were quantitated using Image Studio Lite (LI-COR Biosciences).
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