Abcam, ab93699, Recombinant human Lactate Dehydrogenase protein (Active)

Size: 100µg / 500µg
Recombinant human Lactate Dehydrogenase protein (Active) is a Human Full Length protein, in the 1 to 332 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, WB, FuncS.
Key facts
Purity:>95% SDS-PAGE,
Expression system:Escherichia coli,
Tags:His tag N-Terminus,
Applications:FuncS, SDS-PAGE, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:Specific activity is > 300 units/mg. in which one unit will convert 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5 at 37°C.Activity Assay,
Accession:P00338,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 20% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl

Product details:
Concentration determined by Bradford assay.

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
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.
Biological function summary
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.
Pathways
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.