epitope mapping near the C-terminus of CUL-5 of human origin
recommended for detection of CUL-5 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
CUL-5 Background Information Cullin proteins comprise a distinct family of mediators that participate in the selective targeting of proteins for ubiquitin (Ub)-mediated proteolysis. Cul-1, which is the mammalian homolog of Cdc53 from yeast, is an integral component of the E3 ubiquitin ligase complex designated SCF. The SCF (Skp1/Cul-1/F-box protein complex) consists of Skp1 associating with both Cul-1 and an F-box protein, such as Skp2, which determines the substrate specificity of the complex. Cul-1 mediated ubiquitination results in the degradation of cell cycle proteins cyclin D, p21 and cyclin E. Another cullin, CUL-3 facilitates the degradation of cyclin E independent of SCF activity, while CUL-2 associates with the tumor suppressing protein VHL and elongin B to form VBC complexes, which structurally resemble the SCF ligase. Proteolysis also occurs by way of CUL-4 associating with Nedd-8, a ubiquitin-like protein, where it too functions as an active component of a multifunctional E3 complex. CUL-5, or vasopressin-activated, calcium-mobilizing protein (VACM-1), is also included in the cullin family as it shares substantial sequence homology with CUL-1.
