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Reagents for your SARS-CoV-2 research
The SARS-CoV-2 coronavirus encodes a papain-like cysteine protease PLpro (NSP3) that cleaves the viral polyprotein, removes the ubiquitin-like protein ISG15 and (with lower activity) Lys48-linked polyubiquitin chains. As PLpro is essential for SARS-CoV-2 replication, it represents a promising target for the development of antiviral drugs. In light of this and to complement our well-known ubiquitin based reagents, we are expanding our portfolio of ISG15 based reagents.
There is the fluorescence polarization assay reagent UbiQ-287 (short name hISG15 FP, Figure 1). This is based on full-length human ISG15 that is linked via an isopeptide bond to a 5-carboxytetramethylrhodamine (TAMRA, exc/emi 550/590 nm) functionalized dipeptide (Figure 1).
In addition, we have UbiQ-127 (Ac-ISG15prox-Rh110MP, Figure 2) as a quenched, fluorescent substrate based on the C-terminal domain of mouse ISG15. Cleavage of the amide bond between the C-terminal Gly and rhodamine110 (Rh110) moiety releases the highly fluorescent Rh110-morpholinecarbonyl (Rh110MP). Overall, UbiQ-127 offers the excellent properties of a quenched Ubl-Rh110X substrate with a very high fluorescence intensity after proteolytic cleavage.
Figure 1. hISG15 FP (UbiQ-073) Figure 2. Ac-ISG15prox-Rh110MP (UbiQ-127)
Below we have listed our current portfolio of ISG15 based reagents:
UbiQ-073: ISG15 FP (activity assay reagent, mouse full-length)
UbiQ-287: hISG15 FP (activity assay reagent, human full-length)
UbiQ-127: Ac-ISG15prox-Rh110MP (activity assay reagent, mouse C-terminal domain)
UbiQ-262: Ac-ISG15prox-VPS (activity-based probe, mouse C-terminal domain)