Recombinant Human CUL3/RBX1 Neddylated Complex Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human CUL3/RBX1 Neddylated Complex Protein, CF Summary

• Additional Information: His10
• Details of Functionality: Typical enzyme concentration to support in vitro conjugation will depend on experimental conditions.
• Source: Spodoptera frugiperda, Sf 21 (baculovirus)-derived human CUL3/RBX1 Complex protein
  Met1 - Ala768 with a N-terminal 10-His tag (CUL3); Met1 - His108 (RBX1)
• Accession #: Q13618.2 (CUL3); P62877.1 (RBX1)
• Protein/Peptide Type: Recombinant Enzymes

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 100 kDa (neddylated CUL3), 12 kDa (RBX1).
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
• Buffer: Supplied as a solution in HEPES, NaCl, DTT and Glycerol.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human CUL3/RBX1 Neddylated Complex Protein, CF

• CUL3/RBX1 Complex

Background

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.  

1. Baek, K., et al. (2020) Nature  578:461.
2. Choo, Y.Y. & T. Hagen (2012) PLos One 7:e41350.
3. Davidge, B., et al. (2019) J. Cell Sci. 132:jcs233049. 
4. Duda, D.M., et al. (2012) Mol. Cell 47:371.
5. Stogios, P.J. et al. (2005) Genome Biol. 6:R82.

Publications for CUL3/RBX1 Complex (E3-436)(3)

Publications using E3-436

• Hoffman, M;Krum, D;Wittrup, KD; Bivalent target-binding bioPROTACs induce potent degradation of oncogenic SHP2 The Journal of biological chemistry 2024-07-30 [PMID: 39089586] (Bioassay, N/A)
• J Sharma, S Mulherkar, UI Chen, Y Xiong, L Bajaj, BK Cho, YA Goo, HE Leung, KF Tolias, M Sardiello Calpain activity is negatively regulated by a KCTD7-Cullin-3 complex via non-degradative ubiquitination Cell Discovery, 2023;9(1):32. 2023 [PMID: 36964131] (Ubiquitination, Human)
• J Sharma, S Mulherkar, UI Chen, Y Xiong, L Bajaj, BK Cho, YA Goo, HE Leung, KF Tolias, M Sardiello Calpain activity is negatively regulated by a KCTD7-Cullin-3 complex via non-degradative ubiquitination Cell Discovery, 2023-03-24;9(1):32. 2023-03-24 [PMID: 36964131] (Ubiquitination, Human)

Bioinformatics

• Uniprot:
  • Q13618.2 (CUL3); P62877.1 (RBX1)()