Product Details
| Alternative Name: | Ring box protein-1, ROC1, Regulator of cullins 1, Ring finger protein 75 |
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| MW: | ~14kDa |
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| Source: | Produced in E. coli BL21 (λDE3). |
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| UniProt ID: | P62877 |
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| Formulation: | Liquid. In 50mM TRIS, pH 8.0, containing 50mM NaCl and 1mM DTT. |
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| Purity: | ≥98% (SDS-PAGE) |
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| Purity Detail: | Purified by nickel sepharose affinity chromatography. |
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| Shipping: | Dry Ice |
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| Short Term Storage: | -80°C |
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| Long Term Storage: | -80°C |
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| Use/Stability: | Stable for at least 12 months after receipt when stored at -80°C. |
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| Handling: | Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C. |
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| Scientific Background: | Cullin-based E3 ligases, such as SCF (Skp1-Cdc53-F-box protein), are a large family of multi-subunit ubiquitin ligases with diverse cellular functions, including the regulation of the cell cycle, of the DNA damage response, and of various transcription factors. These ligases are composed of one of six mammalian cullin homologs (Cul1, Cul2, Cul3, Cul4a, Cul4b, and Cul5), the Ring finger containing protein Rbx1/Roc1, and cullin homolog-specific adaptor and substrate recognition subunits. Activation of cullin-based ligases require the covalent modification of a conserved lysine residue in the cullin protein with the ubiquitin-like protein NEDD8. This modification is catalyzed by the Rbx1 subunit. |
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| Regulatory Status: | RUO - Research Use Only |
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Figure: SDS-PAGE image of Rbx1, N-terminally His
6 tagged (Coomassie blue stained). Lane 1: MW markers (top to bottom) 200, 116, 97, 66, 55, 45, 36, 29, 24, 20, 14.2, 6.5 kDa. Lane 2: Rbx1 (human) (recombinant) (His) (Prod. No.
BML-UW0395) (2 µg)."
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General Literature References
Substrate-mediated regulation of cullin neddylation: E.H. Chew & T. Hagen; J. Biol. Chem.
282, 17032 (2007),
Abstract;
A hitchhiker’s guide to the cullin ubiquitin ligases: A.R. Willems, et al.; Biochim. Biophys. Acta
1695, 133 (2004),
Abstract;
Nedd8 on cullin: building an expressway to protein destruction: Z.Q. Pan, et al.; Oncogene
23, 1985 (2004),
Abstract;
