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 .
Anti sumo antibody
Manufactured by GenScript
The anti-SUMO antibody is a laboratory reagent used to detect and identify SUMO (Small Ubiquitin-like Modifier) proteins in various biological samples. SUMO is a post-translational modification that plays a crucial role in regulating protein function, localization, and stability. The anti-SUMO antibody can be used in techniques such as Western blotting, immunoprecipitation, and immunocytochemistry to study the expression and distribution of SUMO proteins in cells and tissues.
Automatically generated - may contain errors
2 protocols using anti sumo 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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