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| Sample Type(s) | Cells etc |
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Overview
For rapid, quantitative, bioluminescent determination of ADP concentration and evaluation of drug effects on ADP metabolism. The assay uses Luminescence for signal readout. Compatible sample input includes Cells etc. Typical stated assay timing is 20 min.
Key elements and design rationale
- Readout format: Luminescence supports plate-based signal acquisition and consistent comparison across matched samples.
- Sample compatibility: The stated sample scope includes Cells etc, which is useful when aligning matrix type with calibration and control design.
- Analytical range context: The supplied specifications include a stated detection limit of 0.02 µM for interpreting low-signal samples.
- Feature emphasis: Safe. Non-radioactive assay.
Additional feature notes highlight Sensitive and accurate. As low as 0.02 µM ADP can be quantified; Homogeneous and convenient. “Mix-incubate-measure” type assay. No wash and reagent transfer steps are involved. Available format information for this listing includes 100 Tests.
Biological background
This product is centered on measurement of enzylight adp within the matrices described for the assay. In practice, datasets from this type of format are typically interpreted by comparing relative signal, activity, or abundance across matched control and experimental groups rather than relying on a single value in isolation. Careful alignment of sample matrix, incubation window, and calibration strategy is important when comparing results across plates, operators, or study days.
More details
BioAssay Systems’EnzyLight™ ADP Assay Kit provides a rapid method to measure ADP levels. The assay involves two steps. In the first step, the working reagent lyses cells to release ATP and ADP. In the presence of luciferase, ATP immediately reacts with the Substrate D-luciferin to produce light. The light intensity is a direct measure of intracellular ATP concentration. In the second step, the ADP is converted to ATP through an enzyme reaction. This newly formed ATP then reacts with the D-luciferin as in the first step. The second light intensity measured represents the total ADP and ATP concentration in the sample. This non-radioactive, homogeneous cell-based assay is performed in microplates. The reagent is compatible with all culture media and with all liquid handling systems for high-throughput screening applications in 96-well and 384-well plates.
Detection method
Luminescence.
Detection limit and analytical sensitivity
Reported detection limit: 0.02 µM.
Procedures and timing
Stated procedure or timing information: 20 min.
Research relevance and current trends
- Plate-based quantification and side-by-side group comparison remain central use cases for this assay format.
- The product notes emphasize multi-sample throughput, making it relevant for screening-oriented and larger batch comparison studies.
- The description supports intervention-focused study designs in which researchers compare baseline and perturbed conditions.
Common research applications
- Quantify enzylight adp in cells by Luminescence readout.
- Compare treatment or phenotype groups using matched cells handling.
- Monitor time-course or pre/post changes in cells across study conditions.
Interpretation is usually strongest when signal changes are assessed alongside matrix-matched controls, replicate agreement, and the assay's stated analytical window.
Notes for experimental interpretation
- Matrix composition, background signal, and sample handling can influence apparent response; compare like-with-like whenever possible.
- Use appropriate blanks, controls, and replicate wells to distinguish biological differences from plate, reagent, or handling variability.
As we know, generally ADP Enzyme was made by myokinase. Then, how the ADP Enzyme as a kit component made?
Our assay does not use adenylate kinase (aka as myokinase), but pyruvate kinase.
For laboratories requiring additional technical capacity, we provide scientific support services including assay execution, method guidance, product sourcing, and customization to align the assay with specific experimental objectives. If you need assistance selecting the appropriate kit configuration, adapting the workflow to your application, or identifying related research services, please click Talk to a Scientist, email support@biohippo.com, or review our Research Services; a member of our scientific team will follow up with recommendations tailored to your study.
Altered energy metabolism during early optic nerve crush injury: Implications of warburg-like aerobic glycolysis in facilitating retinal ganglion cell survival
Zhu, J et al. (2020). Altered energy metabolism during early optic nerve crush injury: Implications of warburg-like aerobic glycolysis in facilitating retinal ganglion cell survival. Neuroscience Bulletin, 36(7): 761-777. Assay: ADP in mouse optical tissue.
Heat shock factor 1 is a direct antagonist of amp-activated protein kinase
Su, KH et al. (2019). Heat shock factor 1 is a direct antagonist of amp-activated protein kinase. Molecular Cell, 76(4): 546-561.e8. Assay: ADP in human cells.
Structural and thermodynamic analyses of interactions between death-associated protein kinase 1 and anthraquinones
Yokoyama, T et al. (2020). Structural and thermodynamic analyses of interactions between death-associated protein kinase 1 and anthraquinones. Acta Crystallographica Section D Structural Biology, 76(5): 438-446. Assay: ADP in human recombinant kinase.
Cryo-EM structures of the ATP-bound Vps4 E233Q hexamer and its complex with Vta1 at near-atomic resolution
Sun, Shan, et al (2017). Cryo-EM structures of the ATP-bound Vps4 E233Q hexamer and its complex with Vta1 at near-atomic resolution. Nature communications 8: 16064. Assay: ADP in yeast cells.
Glyoxylate cycle and metabolism of organic acids in the scutellum of barley seeds during germination
Ma, Zhenguo, et al (2016). Glyoxylate cycle and metabolism of organic acids in the scutellum of barley seeds during germination. Plant Science 248: 37-44. Assay: ADP in barley seeds.
Nitric oxide and reactive oxygen species mediate metabolic changes in barley seed embryo during germination
Ma, Zhenguo, et al (2016). Nitric oxide and reactive oxygen species mediate metabolic changes in barley seed embryo during germination. Frontiers in plant science 7: 138. Assay: ADP in barley seeds.
Hepatic Lipase Release is Inhibited by a Purinergic Induction of Autophagy
Cynthia C, Daniel S (2014). Hepatic Lipase Release is Inhibited by a Purinergic Induction of Autophagy. Cell Physiol Biochem 2014;33:883-894. Assay: ADP in human cell.
Astrocytic Adenosine 5′-Triphosphate Release Regulates the Proliferation of Neural Stem Cells in the Adult Hippocampus
Cao X, Li LP et al(2013). Astrocytic Adenosine 5′-Triphosphate Release Regulates the Proliferation of Neural Stem Cells in the Adult Hippocampus. Stem Cells. 31(8):1633-43. Assay: ADP in human cells.
Mechanisms of hemolysis-associated platelet activatin
Helms CC1, Marvel M et al (2013). Mechanisms of hemolysis-associated platelet activatin. J Thromb Haemost. 11(12):2148-54. Assay: ADP in rodent red blood cell.
Methods For Treatment Of Metabolic Disorders Using Epimetabolic Shifters, Multidimensional Intracellular Molecules, Or Environmental Influencers
Narain, NR (2011). Methods For Treatment Of Metabolic Disorders Using Epimetabolic Shifters, Multidimensional Intracellular Molecules, Or Environmental Influencers. US 2011/0020312 Al. Assay: ADP in mouse cell.
P2X7 receptors mediate deleterious renal epithelial-fibroblast cross talk
Ponnusamy M, et al (2011). P2X7 receptors mediate deleterious renal epithelial-fibroblast cross talk. Am J Physiol Renal Physiol. 300(1):F62-70. Assay: ADP in human epithelial cells.
Anti-ATP Synthase Autoantibodies from Patients with Alzheimer’s Disease Reduce Extracellular HDL Level
Vacirca D, et al (2011). Anti-ATP Synthase Autoantibodies from Patients with Alzheimer’s Disease Reduce Extracellular HDL Level. J Alzheimers Dis. 26(3):441-5. Assay: ADP in human neuronal cells.
Role of purinergic signaling pathways in V-ATPase recruitment to apical membrane of acidifying epididymal clear cells
Belleannee C, et al (2010). Role of purinergic signaling pathways in V-ATPase recruitment to apical membrane of acidifying epididymal clear cells. Am J Physiol Cell Physiol. 298(4):C817-30. Assay: ADP in human epididymal cells.
Inhibitory effects of adenine nucleotides on brain mitochondrial permeability transition Neurochem Res
Saito A, Castilho RF (2010). Inhibitory effects of adenine nucleotides on brain mitochondrial permeability transition Neurochem Res.35(11):1667-74. Assay: ADP in mouse brain tissue.
