QuantiChrom™ ATPase/GTPase Assay KitQuantiChrom™ ATPase/GTPase Assay Kit
Move your mouse over image or click to enlarge

QuantiChrom™ ATPase/GTPase Assay Kit

For quantitative determination of ATPase, GTPase or any enzyme activity that liberated free phosphate and high-throughput screen for their inhibitors.

• High sensitivity: detection of 0.007 U/L ATPase or GTPase activity.

• Fast and convenient: single reagent, homogeneous "mix-and-measure" assay allows quantitation of enzyme activity within 30 minutes. 

• Robust and amenable to HTS: detection at 620nm greatly reduces potential interference by colored compounds. Z’ factors of >0.7 are observed in 96-well and 384-well plates. Can be readily automated on HTS liquid handling systems.

ATPases and GTPases catalyze the decomposition of ATP or GTP into ADP or GDP and free phosphate ion. These enzymes play key roles in transport, signal transduction, protein biosynthesis and cell differentiation. BioAssay Systems’ QuantiChrom™ ATPase/GTPase Assay Kit offers a highly sensitive method for determining ATPase/GTPase activities in a microplate format. Its proprietary formulation features a single reagent for accurate determination of enzyme activity in 30 min at room temperature. The improved malachite green reagent forms a stable dark green color with liberated phosphate, which is measured on a plate reader (600 - 660 nm).

Cat# Size Price Qty Buy
DATG-200 200 Tests £279.65

Additional Information

Property Value or Rating
Product Size 200 Tests
Manufacturer BioAssay Systems
Applications For quantitative determination of ATPase, GTPase or any enzyme activity that liberated free phosphate and high-throughput screen for their inhibitors.
Method OD620nm
Samples ATPase and GTPase
Species All
Detection Limit 0.007 U/L
Storage 4°C
Shelf Life 12 months
References Assay: ATPase/GTPase in Bacteria ATPase (B. burgdorferi) (Pubmed).

2. Hussey, GS et al (2011). Identification of an mRNP complex regulating tumorigenesis at the translational elongation step. Mol Cell. 41(4):419-31. Assay: ATPase/GTPase in Human GTPase (Pubmed).

3. Binder, M et al (2011). Molecular Mechanism of Signal Perception and Integration by the Innate Immune Sensor Retinoic Acid-inducible Gene-I (RIG-I). J Biol Chem. 286(31):27278-87. Assay: ATPase/GTPase in Human purified protein (Pubmed).

4. Sheikha, GA et al (2010). Some sulfonamide drugs inhibit ATPase activity of heat shock protein 90: investigation by docking simulation and experimental validation. J Enzyme Inhib Med Chem. 2010 Dec 29. [Epub ahead of print]. Assay: ATPase/GTPase in Human Hsp90 inhibition (Pubmed).

5. Bertol, JW et al (2011). Antiherpes activity of glucoevatromonoside, a cardenolide isolated from a Brazilian cultivar of Digitalis lanata. Antiviral Res. 2011 Jul 7. [Epub ahead of print]. Assay: ATPase/GTPase in Monkey Vero cell line, Na(+)K(+)ATPase (Pubmed).

6. Hu, WW et al (2009). Digoxigenin modification of adenovirus to spatially control gene delivery from chitosan surfaces. J Control Release. 135(3):250-8. Assay: ATPase/GTPase in N/A ATPase extract (Pubmed).

" title="

1. Suematsu, T et al (2010). A bacterial elongation factor G homologue exclusively functions in ribosome recycling in the spirochaete Borrelia burgdorferi. Mol Microbiol. 75(6):1445-54. Assay: ATPase/GTPase in Bacteria ATPase (B. burgdorferi) (Pubmed).

2. Hussey, GS et al (2011). Identification of an mRNP complex regulating tumorigenesis at the translational elongation step. Mol Cell. 41(4):419-31. Assay: ATPase/GTPase in Human GTPase (Pubmed).

3. Binder, M et al (2011). Molecular Mechanism of Signal Perception and Integration by the Innate Immune Sensor Retinoic Acid-inducible Gene-I (RIG-I). J Biol Chem. 286(31):27278-87. Assay: ATPase/GTPase in Human purified protein (Pubmed).

4. Sheikha, GA et al (2010). Some sulfonamide drugs inhibit ATPase activity of heat shock protein 90: investigation by docking simulation and experimental validation. J Enzyme Inhib Med Chem. 2010 Dec 29. [Epub ahead of print]. Assay: ATPase/GTPase in Human Hsp90 inhibition (Pubmed).

5. Bertol, JW et al (2011). Antiherpes activity of glucoevatromonoside, a cardenolide isolated from a Brazilian cultivar of Digitalis lanata. Antiviral Res. 2011 Jul 7. [Epub ahead of print]. Assay: ATPase/GTPase in Monkey Vero cell line, Na(+)K(+)ATPase (Pubmed).

6. Hu, WW et al (2009). Digoxigenin modification of adenovirus to spatially control gene delivery from chitosan surfaces. J Control Release. 135(3):250-8. Assay: ATPase/GTPase in N/A ATPase extract (Pubmed).

" target="_blank">

1. Suematsu, T et al (2010). A bacterial elongation factor G homologue exclusively functions in ribosome recycling in the spirochaete Borrelia burgdorferi. Mol Microbiol. 75(6):1445-54. Assay: ATPase/GTPase in Bacteria ATPase (B. burgdorferi) (Pubmed).

2. Hussey, GS et al (2011). Identification of an mRNP complex regulating tumorigenesis at the translational elongation step. Mol Cell. 41(4):419-31. Assay: ATPase/GTPase in Human GTPase (Pubmed).

3. Binder, M et al (2011). Molecular Mechanism of Signal Perception and Integration by the Innate Immune Sensor Retinoic Acid-inducible Gene-I (RIG-I). J Biol Chem. 286(31):27278-87. Assay: ATPase/GTPase in Human purified protein (Pubmed).

4. Sheikha, GA et al (2010). Some sulfonamide drugs inhibit ATPase activity of heat shock protein 90: investigation by docking simulation and experimental validation. J Enzyme Inhib Med Chem. 2010 Dec 29. [Epub ahead of print]. Assay: ATPase/GTPase in Human Hsp90 inhibition (Pubmed).

5. Bertol, JW et al (2011). Antiherpes activity of glucoevatromonoside, a cardenolide isolated from a Brazilian cultivar of Digitalis lanata. Antiviral Res. 2011 Jul 7. [Epub ahead of print]. Assay: ATPase/GTPase in Monkey Vero cell line, Na(+)K(+)ATPase (Pubmed).

6. Hu, WW et al (2009). Digoxigenin modification of adenovirus to spatially control gene delivery from chitosan surfaces. J Control Release. 135(3):250-8. Assay: ATPase/GTPase in N/A ATPase extract (Pubmed).

Related Documents