Anti-Lactate Dehydrogenase B/LDH-B antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

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.

Associated diseases and disorders

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.