Lactate Dehydrogenase, LDH.
Lactate dehydrogenase (LDH) is an enzyme(EC184.108.40.206) 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.
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:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
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.
Title: UDP-N-Acetylglucosamine 2-Epimerase/N-Acetylmannosamine Kinase (GNE)
Binds to Alpha-Actinin 1: Novel Pathways in Skeletal Muscle?
Publications: PLoS One 3.6 (2008): e2477.
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