Recombinant Human CUL3/NEDD8/RBX2 Complex Protein, CF Summary
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins.Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration.The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard.In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
E3-431
| Formulation | X mg/ml (XμM) in 50 mM HEPES pH 7.5, 200 mM NaCl, 10% (v/v) Glycerol, 1 mM DTT |
| Shipping | The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: CUL3/NEDD8/RBX2
Cullin-3 (CUL3) is a core component of multiple BCR (BTB-CUL3-RBX) E3 Ubiquitin ligase complexes that mediate the ubiquitination of several classes of signaling and structural proteins. In the BCR complex, CUL3 serves as a scaffold that organizes one or more BTB (BR-C, Ttk and Bab, also known as a POZ domain) substrate recognition subunits with the RBX subunit and contributes to catalysis through positioning of the substrate and an E2 ubiquitin-conjugating enzyme. Substrate specificity of a BCR ligase is determined by the BTB domain protein(s) associated with the ligase, though BTB-independent CUL3 ligase activity has been reported. In vivo, the E3 ubiquitin ligase of the BCR complex is dependent on neddylation of the cullin subunit, though neddylation may be dispensable for some in vitro reactions. This complex consists of an N-terminal 10-His tagged CUL3 (UniProt Q13618) and untagged RBX2 (UniProt Q9UBF6). CUL3 is neddylated in this complex.
- Baek K., et al. (2020) Nature578: 461
- Choo Y.Y & Hagen T. (2012) PLoS One doi:10.1371/journal.pone.0041350
- Davidge B., et al. (2019) J. Cell Sci. doi: 10.1242/jcs.233049
- Duda D.M., et al. (2012) Mol. Cell 47: 371
- Stogios P.J. et al. (2005) Genome Biol. 6: R82
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