Lactate Dehydrogenase, LDH.

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 interconversion of pyruvateand lactate with concomitant interconversion 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.

The DNA encoding chicken LDH-B is cloned from cDNA library of chicken heart.

Escherichia Coli.

Sterile lyophilized powder.

The protein (1 mg/ml) was lyophilized with 0.1mg potassium phosphate.

It is recommended to reconstitute the lyophilized LDH in sterile 18MΩ-cm H2O not less than 100 μg/ml, which can then be further diluted to other aqueous solutions.

Lyophilized Lactate Dehydrogenase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LDH should be stored at 4°C between 2-7 days and for future use below -18°C.
Please prevent freeze-thaw cycles.

Greater than 95.0% as determined by:

The specific activity was found to be 258 U/mg protein.

One unit is defined as 1umol of NAD+ production per minute under the assay conditions (25°C, pH 7.0). Both transaminase activities include a-hydroxyglutarate dehydrogenase activity.

Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.