Abcam, ab96765, Recombinant human Lactate Dehydrogenase B/LDH-B protein

Size: 100µg / 500µg
Recombinant human Lactate Dehydrogenase B/LDH-B protein is a Human Full Length protein, in the 1 to 334 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.
Key facts
Purity:>95% SDS-PAGE,
Expression system:Escherichia coli,
Tags:His tag N-Terminus,
Applications:SDS-PAGE, Mass SpecSee 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:P07195,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

Product details:
Previously labelled as Lactate Dehydrogenase B.

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 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.