Description
Key facts
Detection method:Colorimetric,
Sample types:Purified protein, Plasma, Tissue Extracts, Cell culture supernatant, Serum, Adherent cells, Cell Lysate,
Reacts with:Goat, Cow, Human,
Assay type:Enzyme activity,
Range:8 - 500 ng/mL,
Assay Platform:Microplate reader
Product details:
The microplate assay ab140361 is used to determine Lactate dehydrogenase B / LDH-B activity (LDHB) in a sample utilizing the immunocapture technique. The specific native LDHB enzyme is immune-captured within the wells of the microplate and activity is determined by following the production of NADH catalyzed by the enzyme. The generation of NADH is coupled to the 1:1 reduction of a reporter dye to yield a colored (yellow) reaction product whose concentration can be monitored by measuring the increase in absorbance at 450 nm (Dye molar extinction coefficient - 37000 M-1 cm-1). The immune-capture based activity assay kit contains all the required reagents for a fast and simple measurement of LDHB activity in a whole cell extract, tissue homogenate, or serum.
Functional lactate dehydrogenase are homo or hetero tetramers composed of M and H protein subunits encoded by the LDHA and LDHB genes, respectively. The major isozymes of skeletal muscle and liver has four muscle (M) subunits; while the main isozymes for heart muscle contains four (H) subunits. The other variants contain both types of subunits. Elevated levels of LDH indicate tissue breakdown in hemolysis. LDH can be used as a marker of myocardial infarction, peaking at days 3 and lasting through day 10. Other disorders indicated by elevated LDH include cancer, meningitis, encephalitis, acute pancreatitis, and HIV. Defects in LDHB are a cause of hereditary LDHB deficiency; however LDHB deficiency is usually asymptomatic.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-Multi, Appropriate long-term storage conditions-Multi, Storage information-Please refer to protocols
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Lactate Dehydrogenase B (LDH-B) also known as LDH is an enzyme that plays an important role in the interconversion of lactate to pyruvate. It belongs to the lactate dehydrogenase family which includes multiple isoenzymes. LDH-B has a molecular weight of approximately 36 kDa and commonly forms a tetramer with three other similar subunits. It is mainly expressed in heart and muscle tissues among others where it functions effectively.
Biological function summary
LDH-B is essential for cellular energy production processes. It catalyzes the conversion of pyruvate a byproduct of glycolysis into lactate while simultaneously converting NADH to NAD+. This reaction is significant under anaerobic conditions where mitochondria-based ATP production is limited. LDH-B does not function alone and can operate as part of the lactate dehydrogenase complex containing different subunit combinations.
Pathways
Lactate and pyruvate metabolism engage LDH-B facilitating the Cori cycle and the lactate shuttle. These pathways enable lactate transport between tissues such as muscle and liver and they are important in maintaining blood glucose levels and energy balance. LDH-B operates alongside its related isoenzymes such as LDH-A which predominantly act in specific tissues and conditions to optimize energy utilization.
Anomalous LDH-B activity associates with conditions like myocardial infarction and some cancer types. Enhanced expression or activity of LDH-B can indicate altered metabolic states in tumors connecting it as a potential marker for certain cancerous conditions. The relationship with other proteins such as the hypoxia-inducible factor (HIF) is notable especially in cancer where HIF can regulate LDH-B expression under low oxygen environments.
