QuantiChrom™ β-N-Acetylglucosaminidase Assay Kit

RT

For quantitatve determination of β -N-Acetylglucosaminidase activity and evaluation of drug modulators. Key Features: Fast and sensitive. Linear detection range (20 µ L sample): 0.2 to 50 U/L for a 30 minute reaction at 37° C. High-throughput. Homogeneous "mix-incubate-measure" type assay. Can be readily automated on HTS liquid handling systems for processing thousands of samples per day. Method: OD405nm. Samples: Urine, serum, plasma, cell lysate, etc. Species: All. Procedure: Assay takes 30 min. Kit size: 100 tests. Detection limit: 0.2 U/L.

Application: ?-N-Acetylglucosaminidase activity determination in biological samples.
Key Features: Fast and sensitive. Linear detection range (20 uL sample): 0.2 to 50 U/L for a 30 minute reaction at 37C.
High-throughput. Homogeneous "mix-incubate-measure" type assay. Can be readily automated on HTS liquid handling systems for processing thousands of samples per day.
Method: OD405nm
Samples: Urine, serum, plasma, cell lysate, etc.
Species: All
Size: 100 tests
Detection Limit: 0.2 U/L
Shelf Life: 12 months
More Details: ?-N-Acetylglucosaminidase (NAG) is a lysosomal enzyme involved in a variety of biological processes such as the degradation of glycoproteins and glycolipids, cell proliferation, and signal transduction. NAG is found in many tissues in the body, but due to its high molecular weight, it can not be filtered through the glomerular membrane. For this reason, in the presence of tubular damage or a glomerular lesion, urinary NAG activity increases. Elevated NAG levels in urine are an early indication of renal damage, such as injury due to diabetes mellitus, inflammation, nephritic syndrome, urinary tract infection, and more. Various forms of cancer have been associated with increased levels of NAG in serum. Genetically inherited lipid storage disorders, such as Tay-Sachs and Sandhoff disease, arise from deficiencies of the enzyme. BioAssay Systems non-radioactive, colorimetric NAG assay is based on the cleavage of p-nitrophenol from a synthetic substrate. p-Nitrophenol becomes intensely colored after addition of the stop reagent. The increase in absorbance at 405 nm after addition of the stop reagent is directly proportional to the enzyme activity.