Product Overview

Cholesterol oxidase (CO) is a recombinant microbial oxidase and serves as the universal core enzyme for comprehensive cholesterol assays, including total cholesterol and high- and low-density lipoprotein cholesterol. It specifically catalyzes the oxidation of free cholesterol to produce hydrogen peroxide and is compatible with the Trinder reaction-based colorimetric system. Produced via high-density microbial fermentation followed by column chromatographic purification, it is manufactured on an industrial scale and supplied with long-term stability. The dry powder exhibits a specific activity of ≥15 U/mg, an exceptionally broad pH tolerance of 4.5-10.0, and thermal stability at 50°C that meets leading international standards. It also demonstrates robust resistance to commonly used nonionic surfactants in cholesterol assay reagents. CO boasts an outstanding enzyme activity half-life, excellent formulation compatibility, and optimal synergistic performance when paired with cholesterol esterase (HH0408) and peroxidase (HH2801). When formulated into HDL-C and LDL-C reagents, it delivers high accuracy comparable to imported Randox quality control materials, with strong anti-interference properties; even after accelerated testing at 37°C for 14 days, its performance remains stable and unchanged. The protein purity of CO is exceptionally high, with rigorously controlled levels of contaminating enzymes, ensuring no interference from exogenous oxidases. It is well suited for largescale contract manufacturing of cholesterol reagents, as well as for developing standardized liquid and dry-strip IVD products for global manufacturers.

Key Features

Tolerance to a wide range of surfactants

It exhibits tolerance to a wide range of surfactants, demonstrates excellent compatibility with multiple cholesterol esterases, and is highly compatible with various cholesterol assay systems.

Incubation at 37℃ for one day

Excellent pH and thermal stability, with guaranteed reagent stability.

Applications

Core Application-Lipid Profile Testing: The core raw material for cholesterol assay reagents, supplied with cholesterol esterase (HH0408) and peroxidase (HH2801), is used in the development and large-scale preparation of high- and low-density lipoprotein cholesterol as well as total cholesterol assays.

Reaction Principle

The amount of quinone imine produced in the reaction can be determined by measuring the absorbance at 555nm using a spectrophotometer. One unit of enzyme activity is defined as the amount of enzyme required to catalyze the formation of 1μmol of H₂O₂ per minute under conditions of pH6.5 and 37°C.

Specification

Available Formats

• HH0504-01 2kU

• HH0504-02 100kU

• HH0504-03 500kU

• HH0504-04 1000kU

• HH0504-99 Customizable

Performance Data

Excellent resistance to common interfering substances

HDL-C reagents exhibit excellent resistance to common interfering substances, with average deviations of measured values before and after acceleration both remaining below ±10%.

HDLC reagent demonstrated good measurement correlation, minimal bias, and stable performance

After 14 days of accelerated testing at 37°C, the HDLC reagent demonstrated good measurement correlation, minimal bias, and stable performance across 40 samples.

Excellent resistance to common interfering substances

LDL-C reagents exhibit excellent resistance to common interfering substances, with average deviations of measured values before and after acceleration both remaining below ±10%.

LDLC reagent demonstrated good measurement correlation, minimal bias, and stable performance

After 14 days of accelerated testing at 37°C, the LDLC reagent demonstrated good measurement correlation, minimal bias, and stable performance across 40 samples.