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With ubiquitin’s core functions in plants and animals being so similar it has long been speculated that insights into the ubiquitin proteasome system for plants could also carry over to animals. The question historically has remained whether or not someone can study the UPS using similar methodology for plants as for animals. Modifications to ubiquitin, or an E3, tags, emitors, and so on can lead to unintended behavior and potential artifacts or false positives in studying targeted protein degradation leading to some doubts in the successful crossover in that methodology. Plants potentially contain upwards of 1,000 E3 ligase compared to animals, and so modifications to the fundamentals of the ubiquitin proteasome system can cast doubt onto the accuracy of studies into plant ubiquitinomics with a focus on targeted protein degradation.
In order to study heat stress in plants (Agrositis stolonifera L) Fan et al. utilized Tandem Ubiquitin Binding Entities (TUBEs) a known research tool for studying natural ubiquitination and applied this development to one of TUBEs other known applications, Mass-Spec proteomics. The specific tool used for this study was a K48 version of LifeSensors’s UM420, a pre-built kit designed for a researcher to preform their own ubiquitinomics study. This kit, internally referred to as UM4820 utilizes a K48 specific TUBE as well as supporting reagents to perform trypsin digestion and then run those enriched samples on mass spec.
The full paper is available here.
With ubiquitin’s core functions in plants and animals being so similar it has long been speculated that insights into the
The functional consequences of protein polyubiquitination are determined by the type of ubiquitin chain assembled on the substrate. Among the
While direct K-RAS inhibitors represent a major therapeutic advance, targeting this oncoprotein remains a significant challenge due to limited druggable
Pan-selective Tandem Ubiquitin-Binding Entities (TUBEs) are engineered, high-affinity reagents composed of multiple ubiquitin-associated (UBA) domains that bind polyubiquitin chains with
LifeSensors is pleased to bring attention to some of our academic colleagues who have used our products in the past
Different lysines on ubiquitin are involved in forming different ubiquitin chains, with K48-linked chains primarily signaling for proteasomal degradation, while
With ubiquitin’s core functions in plants and animals being so similar it has long been speculated that insights into the
The functional consequences of protein polyubiquitination are determined by the type of ubiquitin chain assembled on the substrate. Among the
While direct K-RAS inhibitors represent a major therapeutic advance, targeting this oncoprotein remains a significant challenge due to limited druggable
Pan-selective Tandem Ubiquitin-Binding Entities (TUBEs) are engineered, high-affinity reagents composed of multiple ubiquitin-associated (UBA) domains that bind polyubiquitin chains with
LifeSensors is pleased to bring attention to some of our academic colleagues who have used our products in the past
Different lysines on ubiquitin are involved in forming different ubiquitin chains, with K48-linked chains primarily signaling for proteasomal degradation, while
