Cromatest

378 results

  • Amylase MR 1x20ml

    Lactate dehydrogenase (LDH) in the presence of reduced nicotinamide adenine dinucleotide (NADH). The reaction is kinetically monitored at 340 nm through the decrease in absorbance resulting from the oxidation of NADH to NAD+, proportional to ALT activity in the sample.

  • Amylase MR 2x30ml

    Lactate dehydrogenase (LDH) in the presence of reduced nicotinamide adenine dinucleotide (NADH). The reaction is kinetically monitored at 340 nm through the decrease in absorbance resulting from the oxidation of NADH to NAD+, proportional to ALT activity in the sample.

  • Amylase MR 8x30ml

    Lactate dehydrogenase (LDH) in the presence of reduced nicotinamide adenine dinucleotide (NADH). The reaction is kinetically monitored at 340 nm through the decrease in absorbance resulting from the oxidation of NADH to NAD+, proportional to ALT activity in the sample.

  • Amylase MR 2x40ml

    Lactate dehydrogenase (LDH) in the presence of reduced nicotinamide adenine dinucleotide (NADH). The reaction is kinetically monitored at 340 nm through the decrease in absorbance resulting from the oxidation of NADH to NAD+, proportional to ALT activity in the sample.

  • AST/GOT BR opt. 3x100ml

    Aspartate aminotransferase (AST/GOT) catalyzes the transfer of the amino group from aspartate to alpha-ketoglutarate, forming glutamate and oxaloacetate. The latter is reduced to malate by malate dehydrogenase (MDH) in the presence of reduced nicotinamide adenine dinucleotide (NADH). The reaction is kinetically monitored at 340 nm by the decrease in absorbance resulting from the oxidation of NADH to NAD+, proportional to AST activity in the sample.

  • AST/GOT BR opt. 5x40ml

    Aspartate aminotransferase (AST/GOT) catalyzes the transfer of the amino group from aspartate to alpha-ketoglutarate, forming glutamate and oxaloacetate. The latter is reduced to malate by malate dehydrogenase (MDH) in the presence of reduced nicotinamide adenine dinucleotide (NADH). The reaction is kinetically monitored at 340 nm by the decrease in absorbance resulting from the oxidation of NADH to NAD+, proportional to AST activity in the sample.

  • AST/GOT BR opt. 11x40ml

    Aspartate aminotransferase (AST/GOT) catalyzes the transfer of the amino group from aspartate to alpha-ketoglutarate, forming glutamate and oxaloacetate. The latter is reduced to malate by malate dehydrogenase (MDH) in the presence of reduced nicotinamide adenine dinucleotide (NADH). The reaction is kinetically monitored at 340 nm by the decrease in absorbance resulting from the oxidation of NADH to NAD+, proportional to AST activity in the sample.

  • AST/GOT BR opt. 3x50ml

    Aspartate aminotransferase (AST/GOT) catalyzes the transfer of the amino group from aspartate to alpha-ketoglutarate, forming glutamate and oxaloacetate. The latter is reduced to malate by malate dehydrogenase (MDH) in the presence of reduced nicotinamide adenine dinucleotide (NADH). The reaction is kinetically monitored at 340 nm by the decrease in absorbance resulting from the oxidation of NADH to NAD+, proportional to AST activity in the sample.

  • Acid Phosphatase 4x10ml

    The method is based on the hydrolysis of a-naphthyl phosphate at pH 5.0 by acid phosphatase (FAC), producing a-naphthol and inorganic phosphate. Pentanediol acts as a phosphate acceptor, increasing the reaction sensitivity. a-naphthol reacts with a diazonium salt, Fast Red TR*, forming a colored complex directly proportional to the FAC activity in the sample.

  • Albumin 2x50ml

    Albumin 2x50ml

    1101000

    The method is based on the specific binding of bromocresol green (VBC), an anionic dye, and the protein at an acidic pH, resulting in a shift in the absorption spectrum of the complex. The intensity of the formed color is proportional to the concentration of albumin in the sample.

  • Albumin 4x100ml

    Albumin 4x100ml

    1101010

    The method is based on the specific binding of bromocresol green (VBC), an anionic dye, and the protein at an acidic pH, resulting in a shift in the absorption spectrum of the complex. The intensity of the formed color is proportional to the concentration of albumin in the sample.

  • Albumin 4x250ml

    Albumin 4x250ml

    1101025

    The method is based on the specific binding of bromocresol green (VBC), an anionic dye, and the protein at an acidic pH, resulting in a shift in the absorption spectrum of the complex. The intensity of the formed color is proportional to the concentration of albumin in the sample.