Rabbit anti-uL23 antibody was customized from GenScript using CGKVKRHGQRIGRRS as the epitope. Anti-T7 antibody was purchased from Abcam. Anti-strep, anti-HA and anti-SUMO antibody were purchased from GenScript. Primary antibodies were incubated with IRDye® 800CW secondary antibodies (LI-COR) for detection. Protein band intensity was quantified by the Odyssey® CLx imaging system. The additional bands in the anti-T7 blots are potentially SecA dimer induced by cysteine-cysteine crosslinking, because: (i) their apparent size (slightly above 200kDa) is consistent with a SecA dimer (204kDa); (ii) their appearance depends on the presence of the crosslinker; (iii) their intensity depends on the position of engineered cysteine on SecA (Fig. 1a and new Supplementary Fig. 1g ), with the strongest band at residue 797 (Fig. 1a ) near a reported SecA dimer interface48 .
Rabbit anti ul23 antibody
Manufactured by GenScript
Rabbit anti-uL23 antibody is a primary antibody that recognizes the uL23 protein, a ribosomal protein component. It is designed for use in various research applications, such as Western blotting and immunohistochemistry, to detect and analyze the uL23 protein in biological samples.
Automatically generated - may contain errors
2 protocols using rabbit anti ul23 antibody
1
Antibody-based Detection of SecA Dimer
2
Antibody-based Detection of SecA Dimer
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Rabbit anti-uL23 antibody was customized from GenScript using CGKVKRHGQRIGRRS as the epitope. Anti-T7 antibody was purchased from Abcam. Anti-strep, anti-HA and anti-SUMO antibody were purchased from GenScript. Primary antibodies were incubated with IRDye® 800CW secondary antibodies (LI-COR) for detection. Protein band intensity was quantified by the Odyssey® CLx imaging system. The additional bands in the anti-T7 blots are potentially SecA dimer induced by cysteine-cysteine crosslinking, because: (i) their apparent size (slightly above 200kDa) is consistent with a SecA dimer (204kDa); (ii) their appearance depends on the presence of the crosslinker; (iii) their intensity depends on the position of engineered cysteine on SecA (Fig. 1a and new Supplementary Fig. 1g ), with the strongest band at residue 797 (Fig. 1a ) near a reported SecA dimer interface48 .
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