Amplite® Colorimetric Asparaginase Activity Assay Kit

Amplite® Colorimetric Asparaginase Activity Assay Kit is a colorimetric assay kit for quantification of asparaginase activity in biological samples.

Detection Principle: Generates a colored product proportional to aspartate produced by asparaginase.
Chemistry: Measures asparaginase activity through conversion of asparagine to aspartate and ammonia.
Signal Response: Absorbance increases in proportion to the amount of aspartate generated by the enzyme reaction.
Instrument Compatibility: Read absorbance at 570 nm using a clear-bottom microplate.
Applications: Suitable for asparaginase activity measurements in biological, biochemical, and biotechnology research.

Aspartate dose responses was measured using the Amplite® Colorimetric Asparaginase Activity Assay Kit on a 96-well clear bottom microplate with a ClarioStar microplate reader (BMG) at 570 nm.

Protocol

SDS

COA

Catalog	Size	Price	Quantity
11800	100 Tests	Price

Overview

The Amplite® Colorimetric Asparaginase Activity Assay Kit provides a simple and straightforward procedure for measuring Asparaginase activity in a variety of biological samples. Asparaginase activity is determined by a coupled enzyme assay, which results in the formation of a colored product with absorbance at 575 nm. The amount of the colored product and the absorbance value is proportional to the aspartate generated by the asparaginase enzyme. One unit (U) is the amount of enzyme that catalyzes the reaction of 1 µmol of substrate per minute. Asparaginase is an essential enzyme catalyzing the hydrolysis of non-essential amino acid Asparagine to Aspartate and Ammonia. It plays a crucial role in cellular functions, particularly in hematopoietic cells which rely on exogenous asparagine for protein synthesis. Asparaginase is found in plants, microorganisms, and certain animals, but does not occur naturally in humans, making it a valuable therapeutic agent in medicine and an essential tool in various industries. Asparaginase is used to treat acute lymphocytic leukemia (ALL) by starving tumor cells of needed nutrients and slowing tumor cell growth. Depletion of circulating asparagine by asparaginase induces cell cycle arrest and apoptosis in malignant cells, offering a targeted approach to cancer treatment. Beyond its medical applications, asparaginase is also used in the food industry to reduce the formation of acrylamide, a potentially carcinogenic compound, in starchy and fried foods. The versatility of this enzyme extends to various research fields, including biotechnology and biochemistry.

References

View all 50 references: Citation Explorer

Enhanced anti-cancer potency of sustainably synthesized anisotropic silver nanoparticles as compared with L-asparaginase.

Authors:

Naqvi, Syed Mohd Adnan and Islam, Sk Najrul and Kumar, Abhishek and Patil, Chandrahas Ramchandra and Kumar, Ajay and Ahmad, Absar

Journal:

International journal of biological macromolecules (2024): 130238

Hyperglycemia and Other Glycemic Measures Throughout Therapy for Pediatric Acute Lymphoblastic Leukemia and Lymphoma.

Authors:

Demedis, Jenna and Scarbro, Sharon and Suresh, Krithika and Maloney, Kelly and Forlenza, Gregory P

Journal:

Journal of pediatric hematology/oncology (2023): e154-e160

Asparaginyl endopeptidase contributes to cetuximab resistance via MEK/ERK signaling in RAS wide-type metastatic colorectal cancer.

Authors:

Xu, Xiaojing and Liu, Mengling and Peng, Ke and Yu, Yiyi and Liu, Tianshu

Journal:

Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Can (2023): 776-785

Asparagine and Glutamine Deprivation Alters Ionizing Radiation Response, Migration and Adhesion of a p53null Colorectal Cancer Cell Line.

Authors:

Guardamagna, Isabella and Iaria, Ombretta and Lonati, Leonardo and Mentana, Alice and Previtali, Andrea and Uggè, Virginia and Ivaldi, Giovanni Battista and Liotta, Marco and Tabarelli de Fatis, Paola and Scotti, Claudia and Pessino, Greta and Maggi, Maristella and Baiocco, Giorgio

Journal:

International journal of molecular sciences (2023)

GSK3α Regulates Temporally Dynamic Changes in Ribosomal Proteins upon Amino Acid Starvation in Cancer Cells.

Authors:

Loxha, Lorent and Ibrahim, Nurul Khalida and Stasche, Anna Sophie and Cinar, Büsra and Dolgner, Tim and Niessen, Julia and Schreek, Sabine and Fehlhaber, Beate and Forster, Michael and Stanulla, Martin and Hinze, Laura

Journal:

International journal of molecular sciences (2023)

Usage and storage

Intended use

Research Use Only (RUO)

Instrument settings

Absorbance microplate reader
Absorbance	570 nm
Recommended plate	Clear bottom

Telephone
Fax
Email	sales@aatbio.com
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Shipping	Standard overnight for United States, inquire for international

Page updated on October 25, 2026

Component A: Amplite® Red Substrate	1 Vial
Component B1: Enzyme Mix1	1 Bottle
Component B2: Enzyme Mix 2	1 Bottle
Component C: Assay Buffer	1 Bottle (5 mL)
Component D: Conversion Mix	1 Vial
Component E: Aspartate Standard	1 Vial
Component F: Asparaginase Positive Control	1 Vial
Component G: DMSO	1 Vial (100 µL)