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Lysine-targeting specificity in ubiquitin and ubiquitin-like modification pathways.

Nature structural & molecular biology (2014-04-05)
Francesca Mattiroli, Titia K Sixma
ABSTRACT

Ubiquitin and ubiquitin-like modifications are central to virtually all cellular signaling pathways. They occur primarily on lysine residues of target proteins and stimulate a large number of downstream signals. The diversity of these signals depends on the type, location and dynamics of the modification, but the role of the exact site of modification and the selectivity for specific lysines are poorly understood. Here we review the current literature on lysine specificity in these modifications, and we highlight the known signaling mechanisms and the open questions that pose future challenges to ubiquitin research.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
L-Lysine monohydrochloride, from non-animal source, meets EP, JP, USP testing specifications, suitable for cell culture, 98.5-101.0%
Sigma-Aldrich
L-Lysine monohydrochloride, reagent grade, ≥98% (HPLC)
Supelco
L-Lysine monohydrochloride, Pharmaceutical Secondary Standard; Certified Reference Material
Sigma-Aldrich
L-Lysine monohydrochloride, BioUltra, ≥99.5% (AT)
Supelco
L-Lysine Acetate, Pharmaceutical Secondary Standard; Certified Reference Material
Lysine hydrochloride, European Pharmacopoeia (EP) Reference Standard
Supelco
L-Lysine monohydrochloride, certified reference material, TraceCERT®
Sigma-Aldrich
L-Lysine monohydrochloride, Vetec, reagent grade, ≥98%
Sigma-Aldrich
L-Lysine, crystallized, ≥98.0% (NT)
Sigma-Aldrich
L-Lysine, Vetec, reagent grade, ≥98%
Lysine acetate, European Pharmacopoeia (EP) Reference Standard
Supelco
L-Lysine, analytical standard
Sigma-Aldrich
L-Lysine, ≥98% (TLC)
Sigma-Aldrich
L-Lysine acetate salt, ≥98% (HPLC)