Lactate Dehydrogenase (LDH) Assay Kit (Fluorometric) (ab197000) provides a quick and easy method for monitoring Lactate Dehydrogenase (LDH) activity in a wide variety of samples.
Individual kit components also available for purchase with a minimum order of 20 units. Contact us to discuss your needs.
Fluorescent
Urine, Plasma, Suspension cells, Tissue Extracts, Cell culture media, Serum, Other biological fluids, Adherent cells
Enzyme activity
Mammals
20m
= 1 µU/mL
Select an associated product type
Lactate Dehydrogenase (LDH) Assay Kit (Fluorometric) (ab197000) provides a quick and easy method for monitoring Lactate Dehydrogenase (LDH) activity in a wide variety of samples.
Individual kit components also available for purchase with a minimum order of 20 units. Contact us to discuss your needs.
Fluorescent
Urine, Plasma, Suspension cells, Tissue Extracts, Cell culture media, Serum, Other biological fluids, Adherent cells
Enzyme activity
Mammals
20m
Microplate reader
= 1 µU/mL
Blue Ice
-20°C
-20°C
-20°C
Lactate Dehydrogenase (LDH) Assay Kit (Fluorometric) (ab197000) provides a quick and easy method for monitoring Lactate Dehydrogenase (LDH) activity in a wide variety of samples. In this assay, LDH converts lactate into pyruvate and NADH, which reacts with the specific fluorescent probe to generate an intense fluorescent product (Ex/Em = 535/587 nm).
This kit is simple, highly sensitive and high-throughput adaptable and can detect LDH activity as low as 1 μU/mL.
LDH assay protocol summary:
- add samples and standards to wells
- add reaction mix
- analyze with microplate reader every 2-3 min for 10-30 min
This product is manufactured by BioVision, an Abcam company and was previously called K730 PicoProbe™ Lactate Dehydrogenase Activity Assay Kit. K730-500 is the same size as the 500 test size of ab197000.
Lactate dehydrogenase (LDH, L-Lactate NAD oxidoreductase, EC 1.1.1.27) is an ubiquitous enzymes among vertebrate organisms which catalyzes the reversible conversion of pyruvate to lactate, with concomitant conversion of NADH and NAD+. LDH is cytoplasmic in its cellular location and in any one tissue is composed of one or two of five possible isoenzymes. During tissue damage, LDH is released into the bloodstream; therefore it serves as a marker for various diseases and common injuries.
This supplementary information is collated from multiple sources and compiled automatically.
Lactate dehydrogenase (LDH) is an enzyme that catalyzes the interconversion of pyruvate and lactate along with the conversion of NADH to NAD+. LDH is known by other names such as lactic acid dehydrogenase and LDH-5. The enzyme has a molecular weight of approximately 36 kDa. LDH exists in almost all tissues having multiple isoforms that are expressed differently depending on the tissue type. It shows high expression in muscle tissue liver and heart indicating its extensive role in energy metabolism.
Lactate dehydrogenase plays a critical role in anaerobic glycolysis. The enzyme helps in regenerating NAD+ from NADH allowing glycolysis to continue in the absence of oxygen. LDH is not a part of any larger protein complex working independently to fulfill its function in the glycolytic pathway. It serves in rapid energy production especially under hypoxic or exertional conditions where oxygen supply is limited.
LDH is significantly involved in the glycolysis and gluconeogenesis pathways. Within glycolysis LDH helps facilitate the conversion of pyruvate to lactate during anaerobic conditions a step important for ATP production when oxygen is scarce. The enzyme is tied closely to phosphofructokinase-1 (PFK-1) in glycolysis given that both enzymes are central to maintaining the glycolytic flow. In gluconeogenesis though functionally reversed from its role in glycolysis LDH helps to manage lactate removal an important step for glucose synthesis from non-carbohydrate sources.
Lactate dehydrogenase levels often act as a biomarker for tissue damage or certain cancers as its release into the bloodstream signals cellular injury or death. Elevated LDH levels are associated with conditions like myocardial infarction and certain forms of anemia. In cancer such as lymphoma or leukemia LDH correlates with the progression of the disease and acts as a prognostic marker. LDH's connection to these conditions often leads to insights into disease severity and progression due to its association with proteins like p53 and HIF-1 which play roles in cellular metabolism and hypoxia response.
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Typical NADH Standard Curve obtained following assay protocol.
Kinetic measurement of Lactate Dehydrogenase activity in a range of biological samples.
Relative LDH Activity was calculated in lysates prepared from rat liver (0.037 μg protein), Jurkat cells (0.053 μg protein), and Human serum (0.2 μg protein).
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