Cullin1 is a core component of the Skp1-Cullin1-F-box (SCF) ubiquitin ligase complex, which plays a pivotal role in the ubiquitin-proteasome system by targeting specific proteins for degradation. As a scaffold protein, Cullin1 facilitates the assembly of the SCF complex, linking the F-box substrate-recognition subunit to the RING-domain protein Rbx1. thereby enabling E3 ubiquitin ligase activity. This activity is critical for regulating diverse cellular processes, including cell cycle progression, signal transduction, and stress responses. Dysregulation of Cullin1-mediated ubiquitination has been implicated in various diseases, such as cancer, neurodegenerative disorders, and immune dysfunction.
Cullin1 antibodies are essential tools for studying the expression, localization, and functional dynamics of Cullin1 in both physiological and pathological contexts. These antibodies are widely used in techniques like Western blotting, immunoprecipitation, and immunofluorescence to detect Cullin1 protein levels, assess its post-translational modifications (e.g., neddylation), or investigate interactions within the SCF complex. High-quality Cullin1 antibodies exhibit specificity for distinct epitopes, enabling researchers to differentiate Cullin1 from other cullin family members. Their applications extend to translational research, including drug development targeting ubiquitination pathways, as modulating SCF activity holds therapeutic potential. Validation of Cullin1 antibodies using knockout controls or siRNA-mediated depletion is crucial to ensure reliability in experimental models, ranging from cell lines to tissue samples.