Lactate Dehydrogenase B Recombinant ( LDHB )

Data sheet

Formulation

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

Solubility

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

Purity

Greater than 95.0% as determined by:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.

Description

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

Protein Background

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 h

Expression host

Escherichia Coli.

Synonyms

Lactate Dehydrogenase, LDH.

Reagent Appearance

Sterile lyophilized powder.

Stability

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.

Unit Definition

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.

Biological Activity

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

References

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. Link: http://journals.plos.org/plosone/articleid=10.1371/journal.pone.0002