immunoprecipitation (IP): 5-10 μg using lysate of rat brain indirect immunofluorescence: 5-10 μg/mL using mouse 3T3 cells western blot: 1-2 μg/mL using whole extract of HEK-293T cells expressing human Cullin 3
Cullin 3 is a member of the cullin family of E3 ubiquitin protein ligases. Cullin 3 forms the BTB-Cul3-Rbx1 (BCR) ubiquitin ligase complex that contains a RING-box protein, Rbx1, and a BTB containing protein. Rbx1 binds to the C-terminus of cullin 3 through its RING-type zinc finger domain to recruit a ubiquitin-conjugating enzyme. The BTB containing protein binds cullin 3 at its N-terminus and functions as a cullin specific adaptor protein.
애플리케이션
Anti-Cullin 3 antibody produced in rabbit has been used in
Cullin 3 (Cul3) acts as a key mediator of post-translational protein regulation. It functions as a scaffold protein that assemble multi-subunit ubiquitin ligase complexes which are responsible for the specific recognition and targeting of substrates for ubiquitin-dependent degradation by the 26S proteasome. Cul3 is required for degradation of the microtubule-severing protein MEI-1/katanin during transitioning from meiosis-to-mitosis phase. It forms a catalytically inactive BTB-Cul3-Rbx1 (BCR) ubiquitin ligase and becomes functional upon covalent attachment of the ubiquitin homologue neural-precursor-cell-expressed. BCR ubiquitin ligase down regulated 8 (Nedd8) near the C terminus of Cul3.
물리적 형태
Solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide.
면책조항
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Many biological processes, such as development and cell cycle progression are tightly controlled by selective ubiquitin-dependent degradation of key substrates. In this pathway, the E3-ligase recognizes the substrate and targets it for degradation by the 26S proteasome. The SCF (Skp1-Cul1-F-box)
Cullin-RING complexes comprise the largest known class of ubiquitin ligases. Owing to the great diversity of their substrate-receptor subunits, it is possible that there are hundreds of distinct cullin-RING ubiquitin ligases in eukaryotic cells, which establishes these enzymes as key
Cullin-based E3 ligases target substrates for ubiquitin-dependent degradation by the 26S proteasome. The SCF (Skp1-Cul1-F-box) and ECS (ElonginC-Cul2-SOCS box) complexes are so far the best-characterized cullin-based ligases. Their atomic structure has been solved recently, and several substrates have been described
Molecular biology of the cell, 18(3), 899-909 (2006-12-29)
Cullins are members of a family of scaffold proteins that assemble multisubunit ubiquitin ligase complexes to confer substrate specificity for the ubiquitination pathway. Cullin3 (Cul3) forms a catalytically inactive BTB-Cul3-Rbx1 (BCR) ubiquitin ligase, which becomes functional upon covalent attachment of