Function
Core component of multiple cullin-RING-based SCF E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. 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. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF and SCF direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF directs ubiquitination of phosphorylated NFKBIA. SCF directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF directs ubiquination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF directs ubiquination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain , and probably PSEN1. SCF directs ubiquitination of GCM1. SCF directs ubiquitination of MYOD1. SCF directs ubiquitination of BIRC2 and DLGAP5. SCF directs ubiquitination of YBX1. SCF does not seem to direct ubiquitination of TP53. SCF mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF directs ubiquitination of CP110.
Storage Buffer
30% Glycerol (glycerin, glycerine), 1% BSA, 68% PBS. pH: 7.40.
