Abcam, ab107922, Asparaginase Activity Assay Kit

Size: 100Test
Asparaginase Activity Assay Kit (Colorimetric/Fluorometric) (ab107922) has one reagent addition step, followed by analysis with a colorimetric plate reader in kinetic mode for 30-60 min.
Key facts
Detection method:Colorimetric/Fluorometric,
Sample types:Cell Lysate,
Assay type:Enzyme activity,
Assay time:40m

Product details:
Asparaginase Activity Assay Kit (Colorimetric/Fluorometric) (ab107922) provides a simple, direct and automation-ready procedure for measuring asparaginase activity in biological samples.
Asparaginase assay principle
In the asparaginase assay protocol, asparaginase hydrolyzes asparagine to generate aspartic acid, which can be detected indirectly colorimetrically (OD=570 nm) or fluorescently (Ex/Em = 535/590 nm) using a coupled enzymatic reaction.
Asparaginase assay protocol summary
- add reaction mix to sample and standard wells and mix
- analyze with microplate reader in kinetic mode for 30-60 min at room temperature
Other notes
This product was previously called K754 Biovision Asparaginase Activity Colorimetric/Fluorometric Assay Kit. Biovision was acquired by Abcam in 2021.
Asparaginase (EC 3.5.1.1) is a homotetramer that catalyzes the hydrolysis of asparagine to aspartic acid and ammonia and exhibits about a 2-4% activity on glutamine and 5% on D-asparagine. Asparaginase does not occur naturally in humans but is found in bacteria, plants and many animals (e.g. guinea pigs).
The Safety Datasheet for this product has been updated for certain countries. Please check the current version in the Support and downloads section.

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information--20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Asparaginase commonly known as L-asparaginase is an enzyme that catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. This enzyme is present in various organisms including bacteria such as Escherichia coli. It is often produced using recombinant methods in strains like E. coli as L-asparaginase or trade names like aspergcel. The molecular mass of L-asparaginase is approximately 135 kDa. It is primarily expressed in microbial cells but is also significant in commercial and medical applications for its enzymatic properties.
Biological function summary
This enzyme plays an important role in the metabolism of amino acids. Unlike humans and some tumor cells normal cells can synthesize L-asparagine while certain types of cancer cells lack this ability and depend on external sources. This dependency makes L-asparaginase an effective therapeutic enzyme as it depletes circulating L-asparagine inhibiting protein synthesis in such tumor cells. The enzyme functions independently and does not typically combine into complex structures.
Pathways
L-asparaginase is involved in the asparagine degradation pathway. This pathway impacts protein synthesis and nitrogen metabolism. When applied therapeutically it interacts indirectly with protein synthesis pathways by reducing the availability of asparagine for cells that cannot synthesize it. Additionally when pegylated PEG-asparaginase it displays enhanced stability and a prolonged circulating half-life providing an efficient effect on target pathways.
Asparaginase is prominently linked to the treatment of acute lymphoblastic leukemia (ALL). Its mechanism to lower asparagine levels starves leukemia cells of necessary nutrients leading to apoptosis. The enzyme is also studied for its potential effects in certain solid tumors that express deficiencies in asparagine synthetase a related protein. Moreover levels of asparaginase activity are often monitored via specialized assays to ensure therapeutic efficacy and manage side effects during treatment.