Anti-Cullin 2/CUL2 Antibody Picoband® Fluoro488 Conjugated

Cullin 2 (CUL2) is a protein that in humans is encoded by the CUL2 gene. Using immunofluorescence, they showed that CUL2 is a cytosolic protein that can be translocated to the nucleus by VHL. By fluorescence in situ hybridization, Clifford et al. (1999) mapped the CUL2 gene to 10p11.2-p11.1, a region reported to show loss of heterozygosity (LOH) in several forms of human cancer, including non-clear cell renal cell carcinoma. Pause et al. (1997) suggested that CUL2 is a candidate tumor suppressor gene, as has been proposed for CUL1 (603134) . Lonergan et al. (1998) demonstrated that formation of the VBC-CUL2 complexes is linked to the regulation of hypoxia-inducible mRNAs by VHL. Cul2 was one of several proteins required for degradation of a class of RNA-binding germline proteins in somatic cells of the early blastomere.

A synthetic peptide corresponding to a sequence in the middle region of human Cullin 2, different from the related mouse and rat sequences by one amino acid.

Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. May serve as a rigid scaffold in the complex and may contribute to catalysis through positioning of the substrate and the ubiquitin- conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (By similarity) . The functional specificity of the ECS complex depends on the substrate recognition component. ECS (VHL) mediates the ubiquitination of hypoxia-inducible factor (HIF) . .

1. Clifford, S. C., Walsh, S., Hewson, K., Green, E. K., Brinke, A., Green, P. M., Gianelli, F., Eng, C., Maher, E. R. Genomic organization and chromosomal localization of the human CUL2 gene and the role of von Hippel-Lindau tumor suppressor-binding protein (CUL2 and VBP1) mutation and loss in renal-cell carcinoma development. Genes Chromosomes Cancer 26: 20-28, 1999. 2. Lonergan, K. M., Iliopoulos, O., Ohh, M., Kamura, T., Conaway, R. C., Conaway, J. W., Kaelin, W. G., Jr.Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2. Molec. Cell. Biol. 18: 732-741, 1998. 3. Pause, A., Lee, S., Worrell, R. A., Chen, D. Y. T., Burgess, W. H., Linehan, W. M., Klausner, R. D. The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins. Proc. Nat. Acad. Sci. 94: 2156-2161, 1997.