Modifying Enzymes
Sigma Aldrich Fine Chemicals Biosciences Catalase from bovine liver lyophilized powder, >=10,000 units/mg protein | 9001-05-2 | MFCD00081483 | 1G
Catalase from bovine liver lyophilized powder, >=10,000 units/mg protein | 9001-05-2 | MFCD00081483 | 1G
XenoTech,LLC Pooled human lung microsomes, non-smokers, mixed gender, 0.5 ML at 10 ME/ML (5 ME)
Pooled human lung microsomes, non-smokers, mixed gender, 0.5 ML at 10 ME/ML (5 ME)
XenoTech,LLC XTreme 200 pool human liver microsomes, mixed gender, 0.5 ML @ 20 ME/ML (10 ME)
XTreme 200 pool human liver microsomes, mixed gender, 0.5 ML @ 20 ME/ML (10 ME)
Sigma Aldrich Fine Chemicals Biosciences Peroxidase from horseradish Type II, essentially salt-free, lyophilized powder, 150-250 units/mg solid (using pyrogallol) | 9003-99-0 | MFCD00071339 | 5ku
Peroxidase from horseradish Type II, essentially salt-free, lyophilized powder, 150-250 units/mg solid (using pyrogallol) | 9003-99-0 | MFCD00071339 | 5ku
Apexbio Technology LLC PreScission Protease (PSP), 200U (1U/uL). Cas: MFCD: NA. Specifically recognize and cleave the Leu-Glu-Val-Leu-Phe-Gln-Gly-Pro peptide in fusion proteins.
PreScission Protease is a fusion protein of human rhinovirus 3C protease and glutothione S trasferase (GST). PreScisson protease can specifically recognize the Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro sequence and cleaves between the Gln and Gly residues. Concentration: 2U/L Other sizes are also available. Please inqury us for quote.
ABclonal Technology Xanthine Oxidase (XDH) Rabbit mAb
Xanthine dehydrogenase belongs to the group of molybdenum-containing hydroxylases involved in the oxidative metabolism of purines. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. Xanthine dehydrogenase can be converted to xanthine oxidase by reversible sulfhydryl oxidation or by irreversible proteolytic modification. Defects in xanthine dehydrogenase cause xanthinuria, may contribute to adult respiratory stress syndrome, and may potentiate influenza infection through an oxygen metabolite-dependent mechanism.