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| Introduction | 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. |
| Synonyms | Lactate Dehydrogenase, LDH. |
| Source | Escherichia Coli. |
| Physical Appearance | Sterile lyophilized powder. |
| Formulation | The protein (1 mg/ml) was lyophilized with 0.1mg potassium phosphate. |
| Solubility | 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. |
| Stability | Lyophilized Lactate Dehydrogenase althoµgh 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. |
| Purity | Greater than 95.0% as determined by(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE. |
| Biological Activity | The specific activity was found to be 258 U/mg protein. |
| Usage | NeoScientific's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drµgs, agricultural or pesticidal products, food additives or household chemicals. |
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