"biosynthesis capping reagent&"
L(+)-Histidine monohydrochloride monohydrate 98.5-101.0% (dried basis), Multi-Compendial, Macron Fine Chemicals™
Supplier: AVANTOR PERFORMANCE MATERIAL LLC
L(+)-Histidine monohydrochloride monohydrate 98.5-101.0% (dried basis), Multi-Compendial, Macron Fine Chemicals™
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L(+)-Histidine monohydrochloride monohydrate 98.5-101.0%, Multi-Compendial, meets analytical specification of ChP, BP, JP, Ph. Eur., Macron Fine Chemicals™
Supplier: AVANTOR PERFORMANCE MATERIAL LLC
L(+)-Histidine monohydrochloride monohydrate 98.5-101.0%, Multi-Compendial, meets analytical specification of ChP, BP, JP, Ph. Eur., Macron Fine Chemicals™
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ß-Nicotinamide adenine dinucleotide phosphate (NADP-Na2, oxidized form) ≥98%, white powder
Supplier: MP Biomedicals
β-NADP is a coenzyme necessary for the alcoholic fermentation of glucose and the oxidative dehydrogenation of other substances. It occurs widely in living tissue, especially in the liver. Nicotinic acid can be converted to nicotinamide in the body and, in this form, is found as a component of two oxidation-reduction coenzymes: nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP). The nicotinamide portion of the coenzyme transfers hydrogens by alternating between oxidized quaternary nitrogen and a reduced tertiary nitrogen. NADP is an essential coenzyme for glucose-6-phosphate dehydrogenase which catalyzes the oxidation of glucose-6-phosphate to 6-phosphogluconic acid. This reaction initiates metabolism of glucose by a pathway other than the citric acid cycle. This route is known as the hexose phosphate shunt or phosphogluconate pathway. Other enzymes which utilize NADP as a coenzyme are: Alcohol dehydrogenase:NADP dependent; Aromatic ADH:NADP dependent; Ferredoxin-NADP reductase; L-Fucose dehydrogenase; Gabase; Galactose-1-phosphate uridyl transferase; Glucose dehydrogenase; L-Glutamic dehydrogenase; Glycerol dehydrogenase:NADP specific; Isocitric dehydrogenase; Malic enzymes; 5,10-Methylenetetrahydrofolate dehydrogenase; 6-Phosphogluconate dehydrogenase and Succinic semialdehyde dehydrogenase.
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VICTOR® Nivo™ Plate Readers, Multi-Mode
Supplier: REVVITY HEALTH SCIENCES, INC.
The VICTOR® Nivo™ system packs all popular detection modes into the industry’s smallest multimode reader footprint. The perfect microplate reader for everyday biochemical assays, cell-based assays, molecular biology and immunoassays. Its software interface is easy to learn and use, and lets you control the instrument from almost any device – perfect for multiuser labs. The VICTOR Nivo is a high-performance multimode microplate reader that can be equipped with all major detection technologies: Absorbance, Luminescence, Fluorescence, Time-Resolved Fluorescence, TR-FRET, Fluorescence Polarization, and Alpha Technology.
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Urea ≥99%, white prills, Ultrapure
Supplier: MP Biomedicals
Urea is the principal end product of nitrogen metabolism in most mammals, formed by the enzymatic reactions of the Kreb's cycle.
Urea is a mild agent usually used in the solubilization and denaturation of proteins. It is also useful for renaturing proteins from samples already denatured with 6 M guanidine hydrochloride such as inclusion bodies; and in the extraction of the mitochondrial complex. It is commonly used to solubilize and denature proteins for denaturing isoelectric focusing and two-dimensional electrophoresis and in acetic acid-urea PAGE gels. Urea is used in cell or tissue culture media to increase the osmolality. Urea has also been used as fertilizer because of the easy availability of nitrogen; in animal feeds; it is reacted with aldehydes to make resins and plastics; condensed with malonic ester to form barbituric acid; used in the paper industry to soften cellulose; used as a diuretic; enhances the action of sulfonamides; an antiseptic.
Urea in solution is in equilibrium with ammonium cyanate. The form that reacts with protein amino groups is isocyanic acid. Urea in the presence of heat and protein leads to carbamylation of the proteins. Carbamylation by isocyanic acid interferes with protein characterization because isocyanic acid reacts with the amino terminus of proteins, preventing N-terminal sequencing. Isocyanic acid also reacts with side chains of lysine and arginine residues resulting in a protein that is unsuitable for many enzymatic digests. In addition, carbamylation often leads to confusing results from peptides having unexpected retention times and masses. When performing enzymatic protein digests it is important to remove urea first. Even though some enzymes will tolerate small amounts of urea, the elevated temperature used for most reactions will lead to carbamylation during the course of the digest. The urea can be removed prior to digestion by fast reversed phase chromatography, spin columns, or dialysis.
Dissolve urea in deionized water to the desired concentration.For every 10 ml of solution, add 1 g of Amberlite® IRA-910.Stir for one hour at room temperature
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Sodium-L(+)-glutamate monohydrate 98.5-101.5% (dry basis) FCC
Supplier: AVANTOR PERFORMANCE MATERIAL LLC
Sodium-L(+)-glutamate monohydrate 98.5-101.5% (dry basis) FCC



