Anti-Cullin-4B antibody produced in rabbit

Cullin-4B forms a complex that functions as an E3 ubiquitin ligase and catalyzes the polyubiquitination of specific protein substrates in the cell. The protein interacts with a ring finger protein, and is required for the proteolysis of several regulators

Mammalian cells express two distinct but highly homologous cullin-4 proteins, cullin-4A and cullin-4B. Cul4A and Cul4B form individual E3 ligases. In contrast to Cul4A, Cul4B has been shown to be localized to the nucleus.

Anti-Cullin-4B antibody produced in rabbit is suitable for western blotting at a working concentration of 0.7-1.5 μg/mL using HEK-293T cells expressing human Cullin-4B. The antibody was used for immunoblotting in a study to demonstrate that CUL4B E3 ubiquitin ligase plays a key role in targeting Jab1 (Jun activation domain-binding protein) for degradation and regulates bone morphogenetic protein signaling.

Cullin-4 (Cul4) proteins are the core components of ubiquitin E3 ligases that regulate cell cycle, genome stability and DNA replication. Cul4B functions as an E3 ligase involved in selecting specific targets for ubiquitylation. It associates with damage-specific DNA binding proteins DDB1 and DDB2 (UV-damaged DNA) and functions as a substrate-recruiting factor for Cul4B E3 ligases. Cul4B ubiquitylates several target proteins including β-catenin, cyclin E, and histone H2A Mutations in this gene has been associated with x-linked mental retardation.

Cullin-4B facilitates the transfer of damaged-DNA binding protein 1 (DDB1) into the nucleus independently of DDB2. In contrast to cullin-4A (Cul4A), cullin-4B (Cul4B) does not ubiquitinate DDB2.

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

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