ab172730 - Rabbit monoclonal IgG, is suitable for use as an isotype control with this antibody.
追加情報Is unsuitable for ICC or IHC-P.
機能Core component of multiple cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein 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 BCR complex depends on the BTB domain-containing protein as the susbstrate recognition component. BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4, H2AFY and DAXX, and probably GLI2 or GLI3. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. Involved in ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in regulation of G1/S transition.
パスウェイProtein modification; protein ubiquitination.
配列類似性Belongs to the cullin family.
翻訳後修飾Neddylated. Attachment of NEDD8 is required for the E3 ubiquitin-protein ligase activity of the BCR complex. Deneddylated via its interaction with the COP9 signalosome (CSN) complex.
Western blot - Anti-Cullin 3 antibody [EPR3195] (ab108407)
All lanes : Anti-Cullin 3 antibody [EPR3195] (ab108407) at 1/5000 dilution
Lane 1 : HeLa cell lysate Lane 2 : SH-SY5Y cell lysate Lane 3 : PC12 cell lysate Lane 4 : NIH 3T3 cell lysate
Lysates/proteins at 10 µg per lane.
Predicted band size : 89 kDa
Anti-Cullin 3 antibody [EPR3195] (ab108407) 使用論文
This product has been referenced in:
Cristini A et al. DNA-PK triggers histone ubiquitination and signaling in response to DNA double-strand breaks produced during the repair of transcription-blocking topoisomerase I lesions. Nucleic Acids Res44:1161-78 (2016).
Read more (PubMed: 26578593) »
Lee J et al. Autophagy suppresses interleukin-1ß (IL-1ß) signaling by activation of p62 degradation via lysosomal and proteasomal pathways. J Biol Chem287:4033-40 (2012).
Read more (PubMed: 22167182) »