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| Product | Description | |
|---|---|---|
| aminoglycoside 2''-phosphotransferase | Requires Mg2+. This bacterial enzyme phosphorylates many 4,6-disubstituted aminoglycoside antibiotics that have a hydroxyl group at position 2'', including kanamycin A, kanamycin B, tobramycin, dibekacin, arbekacin, amikacin, gentamicin C, sisomicin and netilmicin. In most, but not all, cases the phosphorylation confers resistance against the antibiotic. Some forms of the enzyme use ATP as a phosphate donor in appreciable amount. The enzyme is often found as a bifunctional enzyme that also catalyses 6'-aminoglycoside N-acetyltransferase activity. The bifunctional enzyme is the most clinically important aminoglycoside-modifying enzyme in Gram-positive bacteria, responsible for high-level resistance in both Enterococci and Staphylococci. Group: Enzymes. Synonyms: aphD (gene name); APH(2''); aminoglycoside (2'') kinase; gentamicin kinase (ambiguous); gentamicin phosphotransferase (ambiguous). Enzyme Commission Number: EC 2.7.1.190. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3023; aminoglycoside 2''-phosphotransferase; EC 2.7.1.190; aphD (gene name); APH(2''); aminoglycoside (2'') kinase; gentamicin kinase (ambiguous); gentamicin phosphotransferase (ambiguous). Cat No: EXWM-3023. |  |
| Phosphatase from Escherichia coli, Recombinant | A phosphatase is an enzyme that removes a phosphate group from its substrate by hydrolysing phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxyl group (see dephosphorylation). This action is directly opposite to that of phosphorylases and kinases, which attach phosphate groups to their substrates by using energetic molecules like ATP. A common phosphatase in many organisms is alkaline phosphatase. Another large group of proteins present in archaea, bacteria, and eukaryote exhibits deoxyribonucleotide and ribonucleotide phosphatase or pyrophosphatase activities that catalyse the decomposition of dNTP/NTP into dNDP/NDP and a free phosphate ... phosphatase is collectively called as protein phosphatase, which removes a phosphate group from the phosphorylated amino acid residue of the substrate protein. Protein phosphorylation is a common posttranslational modification of protein catalyzed by protein kinases, and protein phosphatases reverse the effect. Group: Enzymes. Synonyms: HAD2. Enzyme Commission Number: EC 3.1.3.-. Purity: >95 % as judged by SDS-PAGE. Phosphatase. Mole weight: 26827.7 Da. Activity: 1.905 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. MG1655. Phosphatase; HAD2; EC 3.1.3.-. Cat No: NATE-1226. | |
| PR-104 | PR-104 is a non-toxic, small-molecule, hypoxia-activated, 3,5-dinitrobenzamide nitrogen mustard pre-prodrug with potential antitumor activity. Upon intravenous administration, PR-104 is converted by systemic phosphatases to the alcohol intermediate PR-104A, which is reduced to form the active DNA-crosslinking mustard species hydroxylamine PR-104H intracellularly under hypoxic conditions. PR-104H specifically crosslinks hypoxic tumor cell DNA, resulting in the inhibition of DNA repair and synthesis, cell-cycle arrest, and apoptosis in susceptible hypoxic tumor cell populations while sparing normoxic tissues. Synonyms: PR 104; PR104; 2- ( (2-Bromoethyl) (2, 4-dinitro-6- ( (2- (phosphonooxy) ethyl) carbamoyl) phenyl) amino) ethyl methanesulfonate; Benzamide, 2-[(2-bromoethyl)[2-[(methylsulfonyl)oxy]ethyl]amino]-3,5-dinitro-N-[2-(phosphonooxy)ethyl]-. Grades: ≥97%. CAS No. 851627-62-8. Molecular formula: C14H20BrN4O12PS. Mole weight: 579.27. |  |
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