1 and 2), supporting the utility of our methodology for quantitative redox profiling in human whole blood samples
The R221G mutation introduces a small noncharged glycine residue that, contrary to the Arg residue cannot form ionic or H-bonds and cannot interact with the WPD-loop Trp179 and Pro180 residues R33A - decreased activity R362K - the Shp2 mutant shows a strongly decreased affinity for the inhibitor phenylhydrazonopyrazolone sulfonate 1 R47V - isoform PTP1B, mutation turns 1B isoform to PTPalpha-like enzyme in substrate recognition R47V/D48N/M258C/G259Q molecular dynamics simulations of the crystal structure, in comparison to wild-type, movement of Q262 is restricted R492L hotspot mutant, dramatically decreased activity despite showing no significant changes in crystal structure S19A site-directed mutagenesis, mutant PTPN12-S19A is efficient in inhibiting EGF-induced cell migration, the mutant does not produce significant differences in PTPN12's recognition of all HER2-phospho-peptides compared to wild-type PTPN12 S19E site-directed mutagenesis, mutant PTPN12-S19E is less efficient in inhibiting EGF-induced cell migration, the mutant does not produce significant differences in PTPN12's recognition of all HER2-phospho-peptides compared to wild-type PTPN12 S270A site-directed mutagenesis, mutation of the catalytic residue in the phosphatase domain, the mutant shows altered enzyme activity kinetic profiles with a synthetic small molecule substrate (pNPP) and the physiological relevant substrate (pERK) when compared to wild-type GST-DUSP5 protein
Third Party Tested Independent third party laboratories verify purity, potency, and accurate dosing to ensure the highest quality and safety standards
10.1016/j.pnpbp.2016.08.008 Prog
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