Product Details
| Alternative Name: | NEDD8-activating enzyme E1 catalytic subunit, NEDD8-activating enzyme E1C, Ubiquitin-activating enzyme E1C, Ubiquitin-like modifier-activating enzyme 3, Ubiquitin-activating enzyme 3 |
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| MW: | 62kDa + 53kDa (heterodimer: 112.15kDa) |
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| Source: | Produced in E. coli. |
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| EC: | 6.3.2.- |
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| UniProt ID: | Q8TBC4 |
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| Formulation: | Liquid. In 25mM HEPES, pH 7.5, containing 150mM NaCl, 1mM DTT. |
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| Purity: | ≥95% (SDS-PAGE) |
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| Purity Detail: | Copurified in His-tagged form with Uba3; copurified with APP-BP1. |
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| Application Notes: | For use in NEDD8 conjugation reactions and NEDDylation pathway studies. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Scientific Background: | Conjugation of mature NEDD8 to specific lysine residues on target proteins via isopeptide bonds allows NEDD8 to play a critical regulatory role in cell proliferation and development, a process closely associated to the ubiquitin-proteasome pathway. An increasing number of substrates for NEDDylation are being identified including the tumor suppressors p53 and VHL and members of the well-characterized cullin ubiquitin E3 ligase family, underlining the vital role NEDD8 modification plays in cellular processes. |
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| Regulatory Status: | RUO - Research Use Only |
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SDS-PAGE Analysis. Lane 1: MW Marker; Lane 2: 1 ug NEDD8 E1.
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Product Literature References
Structural basis for HIV-1 antagonism of host
APOBEC3G via Cullin E3 ligase: F. Ito, et al.; Sci. Adv.
9, eade3168 (2023),
Abstract;
Structural basis for HIV-1 antagonism of host APOBEC3G via Cullin E3 ligase: F. Ito, et al.; Sci. Adv.
9, eade3168 (2023),
Abstract;
Reconstitution of the destruction complex defines roles of AXIN polymers and APC in β-catenin capture, phosphorylation, and ubiquitylation: M. Ranes, et al.; Mol. Cell
81, 3246 (2021),
Abstract;
