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Conditions of optimal lldD 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.
Phone: 1-617-401-8149
Fax: 1-617-606-5019
Email: message@sydlabs.com
Or leave a message with a formal purchase
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Introduction
L-lactate dehydrogenase (lldD) is present in a various organisms, including plants and animals. lldD is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concurrent interconversion of NADH and NAD+. Seeing that lldD can catalyze the oxidation of hydroxybutyrate, it is occasionally called Hydroxybutyrate Dehydrogenase (HBD).
BP002522-ENZ-618: Recombinant E.Coli L-Lactate Dehydrogenase (lldD) Enzyme
Source: E. coli-derived.
A single, non-glycosylated polypeptide chain containing 420 amino acids (1-396) and having a molecular mass of 45.3 kDa. lldD is fused to a 24 amino acid His-tag at N-terminus.
Purity: > 90% as determined by SDS-PAGE.
Formulation: The lldD solution (1 mg/ml) contains 20 mM Tris-HCl buffer (pH8.0), 10% glycerol and 1 mM DTT.
Shipping: The product is shipped with ice pack. 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.
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