| Field | Specification |
|---|---|
| Mfr No | |
| Assay Time | |
| Detection Method | |
| Product Type | |
| Sample Type(s) | Biological samples (e.g. plasma, serum, erythrocytes, tissue, and culture media) |
| Shipping | |
| Species | |
| Storage |
Overview
For quantitative determination of L-malate dehydrogenase enzyme activity and drug effects on malate dehydrogenase metabolism. The assay uses OD565nm for signal readout. Compatible sample input includes Biological samples (e.g. plasma, serum, erythrocytes, tissue, and culture media). Typical stated assay timing is 30 min.
Key elements and design rationale
- Readout format: OD565nm supports plate-based signal acquisition and consistent comparison across matched samples.
- Sample compatibility: The stated sample scope includes Biological samples (e.g. plasma, serum, erythrocytes, tissue, and culture media), which is useful when aligning matrix type with calibration and control design.
- Analytical range context: The supplied specifications include a stated detection limit of 0.5 U/L for interpreting low-signal samples.
- Feature emphasis: Fast and sensitive. Linear detection range (20 µL sample): 0.5 to 65 U/L for 20 min reaction at 37°C.
Additional feature notes highlight Convenient and high-throughput. Homogeneous “mix-incubate-measure” type assay. Can be readily automated on HTS liquid handling systems for processing thousands of samples per day. Available format information for this listing includes 100 Tests.
Biological background
This product is centered on measurement of malate dehydrogenase 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
Malate dehydrogenase (MDH) (EC 1.1.1.37) is an enzyme that reversibly catalyzes the oxidation of L-malate to oxaloacetate in the presence of NAD. There are 2 isoforms in eukaryotic cells: MDH1 and MDH2. MDH1 is found in the cytoplasm and plays a key part in the malate-aspartate shuttle for transporting malate into the mitochondria. MDH2 is a mitochondrial enzyme that participates in the TCA cycle that reversibly converts L-malate into oxaloacetate. Higher MDH activities are found in some neurodegenerative diseases such as Alzheimer’s disease. BioAssay Systems’ non-radioactive, colorimetric MDH assay is based on the reduction of the tetrazolium salt MTT in an NADH-coupled enzymatic reaction to a reduced form of MTT which exhibits an absorption maximum at 565 nm. The increase in absorbance at 565 nm is proportional to the enzyme activity.
Detection method
Colorimetric (OD 565 nm).
Detection limit and analytical sensitivity
Reported detection limit: 0.5 U/L.
Procedures and timing
Stated procedure or timing information: 30 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 malate dehydrogenase in plasma, serum, erythrocytes by OD565 nm readout.
- Compare treatment or phenotype groups using matched plasma, serum, erythrocytes handling.
- Monitor time-course or pre/post changes in plasma, serum, erythrocytes 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.
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.
Implications of lysine acetylation on the enzymes of the tca cycle
Venkat, S. (2020). Implications of lysine acetylation on the enzymes of the tca cycle. Theses and Dissertations. Assay: Malate Dehydrogenase in purified malate dehydrogenase.
Genetically encoding thioacetyl-lysine as a non-deacetylatable analog of lysine acetylation in Escherichia coli
Venkat, S. et al (2017). Genetically encoding thioacetyl-lysine as a non-deacetylatable analog of lysine acetylation in Escherichia coli. FEBS open bio, 7(11), 1805-1814. Assay: Malate dehydrogenase in E.coli cell lysate.
Gan, Q, Lehman, BP, Bobik, TA and Fan, C ( 2016) Expanding the genetic code of Salmonella with non-canonical amino acids
Gan, Q, Lehman, BP, Bobik, TA and Fan, C ( 2016) Expanding the genetic code of Salmonella with non-canonical amino acids. Sci Rep 6, 39920. Assay: Malate dehydrogenase in Salmonella cell lysate.
rationally evolving tRNAPyl for efficient incorporation of noncanonical amino acids
Fan, C et al (2015). rationally evolving tRNAPyl for efficient incorporation of noncanonical amino acids. Nucl. Acids Res. 43(22):e156. Assay: Malate dehydrogenase in E.coli cells.
Adaptation of oxidative phosphorylation to photoperiod-induced seasonal metabolic states in migratory songbirds
Trivedi, AK et al (2015). Adaptation of oxidative phosphorylation to photoperiod-induced seasonal metabolic states in migratory songbirds. Comp. Biochem. Physiol. A 184: 34-40. Assay: Malate dehydrogenase in avian plasma.
