Immunoblotting Protocols for Protein Analysis

The 5-kDa and 9-kDa small proteins were separated on 13% Tris-Tricine polyacrylamide gels. Proteins of molecular weight larger than 20-kDa were analyzed with 12% Tris-Glycine polyacrylamide gels, and then processed for immunoblotting, following the protocols described before [12 (link),28 (link),32 (link)]. Primary antibodies used included anti-GFP (Thermo, Waltham, MA, USA), anti-LIYV CP, anti-LIYV P26, anti-LIYV P5, anti-LIYV P9, and anti-BiP (Agrisera, Vännäs, Sweden) protein polyclonal antibodies produced in rabbit. The secondary antibody was horseradish peroxidase-conjugated goat anti-rabbit IgG.

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Qiao W., Helpio E.L, & Falk B.W. (2018). Two Crinivirus-Conserved Small Proteins, P5 and P9, Are Indispensable for Efficient Lettuce infectious yellows virus Infectivity in Plants. Viruses, 10(9), 459.

Publication 2018

anti-GFP anti-BiP

Anti igg Antibodies Antibody Glycine Goat Horseradish peroxidase Polyacrylamide gels Protein Rabbit Tricine Tris

Corresponding Organization : University of California, Davis

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Variable analysis

independent variables

Protein separation method (13% Tris-Tricine polyacrylamide gels for 5-kDa and 9-kDa proteins, 12% Tris-Glycine polyacrylamide gels for proteins larger than 20-kDa)

dependent variables

Molecular weight of proteins

control variables

Immunoblotting protocol (following previously described protocols in references [12], [28], and [32])
Primary antibodies (anti-GFP, anti-LIYV CP, anti-LIYV P26, anti-LIYV P5, anti-LIYV P9, and anti-BiP)
Secondary antibody (horseradish peroxidase-conjugated goat anti-rabbit IgG)

controls

Positive controls: not specified
Negative controls: not specified

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