Urease
Urease Recombinant
Cat. No.
BT27828
Source
Escherichia Coli.
Synonyms
Appearance
Sterile Lyophilized Powder.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs 
In Stock 
Description
The mutant Urease from microorganism source, showing shifted substrate affinity to urea. It was designed wildtype coding gene from microorganism.
The subunit structure is very similar to well known microbial urease.
Please refer to published literature such as JBC 262, 5963-67 (1987).
It is composed of multi-subunits and shows a bit complex protein structure (alpha 2 Beta 4 Gamma 4) as compared to plant urease
rUrease is genetically designed unique mutant having shifted high Km to urea, which is suited material to kinetic urea assay with wide measurable range.
The enzyme comprises of three different subunits to make complete fully active form, 60.3 kD a subunit, 11.7 kD b subunit and 11.1 kD g subunit respectively.
Product Specs
Description
This engineered Urease enzyme is derived from a microorganism and exhibits altered substrate affinity for urea compared to its wild-type counterpart. The genetic design of this enzyme originates from the wild-type gene found in the microorganism. Structurally, it shares similarities with well-characterized microbial ureases. For a deeper understanding, refer to published studies such as JBC 262, 5963-67 (1987). This urease comprises multiple subunits, forming a slightly intricate protein structure (α2β4γ4) in contrast to plant ureases. Notably, this genetically modified mutant urease (rUrease) displays a distinctive shift towards a higher Km for urea, making it well-suited for kinetic urea assays with an extended measurable range. The enzyme is composed of three distinct subunits (60.3 kDa α subunit, 11.7 kDa β subunit, and 11.1 kDa γ subunit) that assemble to form the fully active enzyme.
Physical Appearance
Lyophilized powder, sterile.
Formulation
Each milligram of protein is formulated with 370 micrograms of Potassium Phosphate and 30 micrograms of EDTA Na2.
Solubility
For reconstitution of the lyophilized Urease, it is advisable to use sterile 18 MΩ-cm H2O.
Stability
While Urease maintains stability at 4°C for a period of 3 weeks, it is recommended to store it in a dry environment below -18°C. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 90.0% as determined by SDS-PAGE analysis.
Unit Definition
One unit of enzyme activity is defined as the amount that catalyzes the oxidation of one micromole of NADH per minute at a temperature of 25°C and a pH of 7.6.
Biological Activity
The measured activity of the enzyme was determined to be 120 units per milligram of powder.
Source
Escherichia Coli.
Product Science Overview
Structure and Function
Urease is a nickel-dependent metalloenzyme, meaning it requires nickel ions to function properly. The enzyme’s active site contains two nickel ions that are essential for its catalytic activity. The structure of urease typically consists of multiple subunits, forming a complex quaternary structure. This multi-subunit arrangement is crucial for the enzyme’s stability and function.
The primary function of urease is to catalyze the breakdown of urea into ammonia and carbon dioxide. This reaction can be represented by the following chemical equation:
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