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RAS GTPases are modified by SUMOylation.

Oncotarget (2018-02-13)
Byeong Hyeok Choi, Changyan Chen, Mark Philips, Wei Dai
RÉSUMÉ

RAS proteins are GTPases that participate in multiple signal cascades, regulating crucial cellular processes including cell survival, proliferation, differentiation, and autophagy. Mutations or deregulated activities of RAS are frequently the driving force for oncogenic transformation and tumorigenesis. Given the important roles of the small ubiquitin-related modifier (SUMO) pathway in controlling the stability, activity, or subcellular localization of key cellular regulators, we investigated here whether RAS proteins are posttranslationally modified (

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Millipore
Nucléase Benzonase®, ≥250 units/μL, ≥90% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous glycerol solution
Sigma-Aldrich
Cocktail d'inhibiteurs de protéases, for use with mammalian cell and tissue extracts, DMSO solution
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Lysozyme from chicken egg white, powder or granules, ≥90 %, ≥39,000 units/mg protein
Sigma-Aldrich
2-D08, ≥98% (HPLC)