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RAS GTPases are modified by SUMOylation.

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

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
Nucleasi® Benzonase, ≥250 units/μL, ≥90% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous glycerol solution
Sigma-Aldrich
Cocktail di inibitori delle proteasi, for use with mammalian cell and tissue extracts, DMSO solution
Sigma-Aldrich
Lisozima, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein
Sigma-Aldrich
2-D08, ≥98% (HPLC)