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Conditions of optimal IDH1 Enzyme performance should be determined experimentally by the investigator.
Price/availability/specifications subject to change without notice. Unless otherwise indicated, our catalog and customized products are for research use only and not intended for human or animal diagnostic or therapeutic use.
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Fax: 1-617-606-5019
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Introduction
Isocitrate Dehydrogenase is an enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle.
BP000574-ENZ-193: Recombinant Human Isocitrate Dehydrogenase-1 (IDH1) Enzyme
Source: E. coli-derived.
A single, non-glycosylated polypeptide chain containing 434 amino acids (1-414) and having a molecular mass of 48.8 kDa. IDH1 is fused to a 20 amino acid His-tag at N-terminus.
The Specific activity is > 0.7 units/ml. One unit will convert 1.0 umole of isocitrate to alpha-ketoglutarate per minute at pH7.5 at 25C.
Purity > 95%, by SDS-PAGE.
Formulation: The IDH1 solution (1 ug/ml) contains 20 mM Tris-HCl buffer (pH 8.0), 0.1 M NaCl, 1 mM DTT, 0.1 mM PMSF and 20% glycerol.
Shipping: The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70°C as supplied.
Other IDH1 Enzymes:
Recombinant Yeast Isocitrate Dehydrogenase-1 Enzyme
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