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SCFSkp2 Complex, Active, Recombinant, Human (SCFSkp2, Skp2/Cks1 complex)

Cat no: 029607


Supplier: United States Biological
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The SCF (Skp1-Cul1-F-box protein) complexes represent the largest family of ubiquitin-protein ligases and mediate the ubiquitination of a broad spectrum of regulatory and signalling proteins in diverse cellular pathways. The SCF consists of three invariant components, Skp1, Cul1 and Rbx1 and an interchangeable subunit, an F-box protein which is responsible for recruiting specific substrates to be ubiquitinated by the SCF. SCFSkp2 mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. It specifically recognizes phosphorylated p27 and is involved in regulation of G1/S transition. Complex formation of SCFSkp2 with Cks1 is required for the degradation of p27. An increased level of Skp2 and reduced level of p27 is linked to poor prognosis in a number of cancers. Source: Recombinant corresponding to complex of N-terminal 6His-tagged, recombinant human Skp2 full length, N-terminal GST-tagged, recombinant human Skp1 full length, N-terminal 6His-tagged, recombinant human Cul1 full length and untagged recombinant human Rbx1 full length, co- expressed by baculovirus in Sf21 insect cells. Molecular Weight: Cks1: ~11kD, Skp2: ~52kD, Skp1: ~46kD, Cul1: ~93kD, Rbx1: ~12kD Storage and Stability: Aliquot to avoid repeated freezing and thawing and store at -70 degrees C. Aliquots are stable for 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Catalogue number: 029607
Size: 10ug
Form: Supplied as a liquid in 50mM Tris/HCl pH7.5, 300mM sodium chloride, 0.1mM EGTA, 0.03% Brij-35, 270mM sucrose, 1mM benzamidine, 0.2mM PMSF, 0.1% 2- mercaptoethanol.
Purity: ~80.8% (SDS-PAGE, Coomassie blue staining)
References: 1. Willems A. R. et al. A Hitchhiker's Guide to the Cullin Ubiquitin Ligases: SCF and its Kin. Biochimica et Biophysica Acta., 1695: 133-170, 2004. 2. Wang W. et al. A Negatively Charged Amino Acid in Skp2 Is Required for Skp2-Cks1 Interaction and Ubiquitination of p27Kip1. J. Biol. Chem., 278: 32390-32396, 2003. 3. Ungermannova D. et al. Ubiquitination of p27Kip1 Requires Physical Interaction with Cyclin E and Probable Phosphate Recognition by SKP2. J. Biol. Chem., 280: 30301-30309, 2005. 4. Xu S. et al. Substrate Recognition and Ubiquitination of SCFSkp2/Cks1 Ubiquitin-Protein Isopeptide Ligase. J. Biol. Chem., 282: 15462-15470, 2007. 5. Xu K. et al. Protein-Protein Interactions Involved in the Recognition of p27 by E3 Ubiquitin Ligase. Biochem. J. 371: 957-964, 2003.

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