Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins . The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit . CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme . Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage . Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication . A number of DCX complexes are part of the DesCEND pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation . The DCX complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D . The DCX complex also acts as a regulator of Cul5-RING E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C component of CRL5 complexes . Required for ubiquitination of cyclin E , and consequently, normal G1 cell cycle progression . Regulates the mammalian target-of-rapamycin pathway involved in control of cell growth, size and metabolism . Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 . With CUL4A, contributes to ribosome biogenesis .

Cullin-4B (CUL-4B)

q13620

Human,Mouse,Rat

WB,IHC

WB 1:1000-1:5000
IHC 1:100-1:200

~104 kD

Rabbit

50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.

Store at -20°C. Stable for 12 months from date of receipt.