DNP-NH-PEG2-C2-acid is a PEG-based linker for PROTACs which joins two essential ligands, crucial for forming PROTAC molecules. This linker enables selective protein degradation by leveraging the ubiquitin-proteasome system within cells.
DNP-NH-PEG4-C2-Boc is a PEG-based linker for PROTACs which joins two essential ligands, crucial for forming PROTAC molecules. This linker enables selective protein degradation by leveraging the ubiquitin-proteasome system within cells.
DNP-PEG3-azide is a PEG-based linker for PROTACs which joins two essential ligands, crucial for forming PROTAC molecules. This linker enables selective protein degradation by leveraging the ubiquitin-proteasome system within cells.
DNP-PEG3-DNP is a PEG-based linker for PROTACs which joins two essential ligands, crucial for forming PROTAC molecules. This linker enables selective protein degradation by leveraging the ubiquitin-proteasome system within cells.
DNP-PEG4-acid is a PEG-based linker for PROTACs which joins two essential ligands, crucial for forming PROTAC molecules. This linker enables selective protein degradation by leveraging the ubiquitin-proteasome system within cells.
DNP-PEG4-alcohol is a PEG-based linker for PROTACs which joins two essential ligands, crucial for forming PROTAC molecules. This linker enables selective protein degradation by leveraging the ubiquitin-proteasome system within cells.
DNP-PEG12-acid is a PEG-based linker for PROTACs which joins two essential ligands, crucial for forming PROTAC molecules. This linker enables selective protein degradation by leveraging the ubiquitin-proteasome system within cells.
DNP-PEG12-NHS ester is a PEG-based linker for PROTACs which joins two essential ligands, crucial for forming PROTAC molecules. This linker enables selective protein degradation by leveraging the ubiquitin-proteasome system within cells.
DNP-PEG4-DBCO is a PEG-based linker for PROTACs which joins two essential ligands, crucial for forming PROTAC molecules. This linker enables selective protein degradation by leveraging the ubiquitin-proteasome system within cells.
DNP-PEG6-acid is a PEG-based linker for PROTACs which joins two essential ligands, crucial for forming PROTAC molecules. This linker enables selective protein degradation by leveraging the ubiquitin-proteasome system within cells.
DNP-PEG6-Boc is a PEG-based linker for PROTACs which joins two essential ligands, crucial for forming PROTAC molecules. This linker enables selective protein degradation by leveraging the ubiquitin-proteasome system within cells.
Dnp-P-Cha-G-Cys(Me)-HA-K(Nma)-NH2 is a fluorogenic substrate for matrix metalloproteinase-1 (MMP-1) and MMP-9. Upon cleavage by MMP-1 or MMP-9, N-methylanthranilic acid (Nma) is unquenched and its fluorescence can be used to quantify MMP activity. Nma displays excitation/emission spectra of 340/440 nm, respectively.
Dnp-PLALWAR is a fluorogenic substrate for matrix metalloproteinase-1 (MMP-1) and MMP-8. The activity of MMP-1 and MMP-8 can be quantified by measuring tryptophan fluorescence that is unquenched upon peptide hydrolysis that removes the N-terminal dinitrophenol (Dnp) group.
Dnp-PLGMWSR is a fluorogenic substrate for matrix metalloproteinase-2 (MMP-2) and MMP-9. The activity of MMP-2 and MMP-9 can be quantified by measuring tryptophan fluorescence that is unquenched upon peptide hydrolysis that removes the N-terminal dinitrophenol (Dnp) group.
Dnp-RPLALWRS is a fluorogenic substrate for matrix metalloproteinase-7 (MMP-7). The activity of MMP-7 can be quantified by measuring tryptophan fluorescence that is unquenched upon peptide hydrolysis that removes the N-terminal dinitrophenol (Dnp) group.
DNP-INT is a quinone analog that inhibits electron transport in plants by competitively inhibiting plastoquinol oxidation by binding at the Qo site of cytochrome b6f (Kd = 1.4 nM). It inhibits electron flow from water to NADP or methylviologen by 50 and 100% when used at concentrations of 0.5 or 5 μM, respectively.
Dnp-PLAYWAR is a fluorogenic substrate for matrix metalloproteinase-8 (MMP-8) and MMP-26. The activity of MMP-8 and MMP-26 can be quantified by measuring tryptophan fluorescence that is unquenched upon peptide hydrolysis that removes the N-terminal dinitrophenol (Dnp) group.
Bacterial Substrate III, Abz/DNP TFA is an internally quenched fluorescent peptide substrate. Staphylococcus aureus transpeptidase sortase A (SrtA) reacts with its native substrate Bacterial Sortase Substrate III, Abz/DNP, cleaving it and catalyzing the f
The Staphylococcus aureus transpeptidase Sortase A (SrtA) anchors virulence and colonization-associated surface proteins to the cell wall. SrtA selectively recognizes a C-terminal LPXTG motif. SrtA readily reacts with its native substrate Abz-LPETG-Dap(DN