Lactate dehydrogenase (LDH) is an enzyme (EC1.1.1.27) present in a wide variety of organisms, including plants and animals. A tetrameric enzyme that catalyses the inter conversion of pyruvate and lactate with concomitant inter conversion of NADH and NAD+. At high concentrations of pyruvate, the enzyme exhibits feedback inhibition and the rate of conversion of pyruvate to lactate is decreased. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.
Source:Recombinant protein corresponding to DNA encoding chicken LDH-B, cloned from cDNA library of chicken heart, expressed in E. coli.
Specific Activity:~200IU/mg
Unit Definition:One unit is defined as 1mol of NAD+ production/minute under the assay conditions (25°C, pH 7.0). Both transaminase activities include alpha-hydroxyglutarate dehydrogenase activity.
Storage and Stability:Lyophilized powder may be stored at -20°C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Reconstituted product is stable for 6 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
仕様
Size：1mg
Source Antigen：Recombinant, E. coli
Grade：Highly Purified
Purity：~95% (RP-HPLC, SDS-PAGE)
Form：Supplied as a lyophilized powder in 0.1mg potassium phosphate. No preservative added. Reconstitute with sterile ddH2O ~100ug/ml.
