Search Results

ACE Hemoglobin A lc (HbA lc) Reagent is intended for the quantitative determination of percent hemoglobin A lc in venous whole blood collected in K2-EDTA tubes using the ACE Axcel® Clinical Chemistry Systems. This test is intended for use in clinical laboratories and physician office laboratories to monitor long term blood glucose control in individuals with diabetes mellitus. For in vitro diagnostic use only.

The ACE Hemoglobin A1c (HbA1c) Reagent assay requires a pretreatment step of denaturation of the whole blood samples, which is performed off-line. The red blood cells in the sample are lysed by the Hemoglobin Denaturant and the hemoglobin chains are hydrolyzed. For determination of HbA1c, a latex agglutination inhibition assay is used. In the absence of HbA1c in the sample, the synthetic polymer containing the immunoreactive portion of HbA 1c Agglutinator Reagent will agglutinate with the antibody-coated microparticles in the HbA1c Antibody Reagent. The presence of HbA1c in the blood sample competes for the antibody binding sites and inhibits agglutination. The increase in absorbance, monochromatically at 692 mm, is inversely proportional to the HbA1c present in the sample. For the determination of total hemoglobin, all hemoglobin derivatives in the sample are converted to alkaline hematin. The reaction produces a green colored solution. which is measured bichromatically at 573 nm/692 nm. The intensity of color produced is directly proportional to the total hemoglobin concentration in the sample. The concentrations of both HbA 1 c and total hemoglobin are measured, the ratio is calculated, and the result reported as percent HbA1c.

The ACE Alkaline Phosphatase Reagent is intended for the quantitative determination of alkaline phosphatase activity in serum and lithium heparin plasma using the ACE, ACE Alera, and ACE Axcel Clinical Chemistry Systems. Measurements of alkaline phosphatase are used in the diagnosis and treatment of liver, bone, parathyroid, and intestinal diseases. This test is intended for use in clinical laboratories and physician office laboratories. For in vitro diagnostic use only. The ACE Amylase Reagent is intended for the quantitative determination of α-amylase activity in serum and lithium heparin plasma using the ACE, ACE Alera, and ACE Axcel Clinical Chemistry Systems. Amylase measurements are used primarily for the diagnosis and treatment of pancreatitis (inflammation of the pancreas). This test is intended for use in clinical laboratories and physician office laboratories. For in vitro diagnostic use only. The ACE ALT Reagent is intended for the quantitative determination of alanine aminotransferase activity in serum and lithium heparin plasma using the ACE, ACE Alera, and ACE Axcel Clinical Chemistry Systems. Alanine aminotransferase measurements are used in the diagnosis and treatment of certain liver diseases (e.g., viral hepatitis and cirrhosis) and heart diseases. This test is intended for use in clinical laboratories and physician office laboratories. For in vitro diagnostic use only. The ACE AST Reagent is intended for the quantitative determination of aspartate aminotransferase activity in serum and lithium heparin plasma using the ACE, ACE Alera, and ACE Axcel Clinical Chemistry Systems. Measurements of aspartate aminotransferase are used in the diagnosis and treatment of certain types of liver and heart disease. This test is intended for use in clinical laboratories and physician office laboratories. For in vitro diagnostic use only.

In the ACE Alkaline Phosphatase Reagent assay, alkaline phosphatase catalyzes the hydrolysis of colorless p-nitrophenyl phosphate to p-nitrophenol and inorganic phosphate. In an alkaline solution (pH 10.5), p-nitrophenol is in the phenoxide form and has a strong absorbance at 408 nm. The rate of increase in absorbance, monitored bichromatically at 408 nm/486 nm, is directly proportional to the alkaline phosphatase activity in the sample. In the ACE Amylase Reagent assay, α-amylase hydrolyzes the 2-chloro-p-nitrophenyl-α-D-maltotrioside substrate to release 2-chloro-p-nitrophenol and form 2-chloro-p-nitrophenyl-α-D-maltoside, maltotriose and glucose. The rate of increase in absorbance, monitored bichromatically at 408 nm/ 647 nm, is directly proportional to the α-amylase activity in the sample. In the ACE ALT Reagent assay, alanine aminotransferase converts the L-alanine and α-ketoglutarate substrates in the reagent to L-glutamate and pyruvate, respectively. Lactate dehydrogenase (LDH) catalyzes the oxidation of the reduced cofactor to the cofactor. The rate of conversion of the reduced cofactor to the cofactor can be determined by monitoring the decrease in absorbance bichromatically at 340 nm/647 nm. This rate of conversion from the reduced cofactor to the cofactor is a function of the activity of ALT in the sample. In the ACE AST Reagent assay, aspartate aminotransferase converts the L-aspartate and α-ketoglutarate in the reagent to oxaloacetate and L-glutamate, respectively. The oxaloacetate undergoes reduction, with concurrent oxidation of NADH to NAD+ in the malate dehydrogenase-catalyzed indicator reaction. NADH absorbs strongly at 340 nm, whereas NAD+ does not. Therefore, the rate of conversion of NADH to NAD+ can be determined by monitoring the decrease in absorbance bichromatically at 340 nm/647 nm. This rate of conversion from NADH to NAD+ is a function of the activity of AST in the sample. Lactate dehydrogenase is added to prevent interference from endogenous pyruvate, which is normally present in blood.